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  • Transfection  (74)
  • American Association for the Advancement of Science (AAAS)  (74)
  • American Chemical Society (ACS)
  • 1990-1994  (74)
  • 1992  (74)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (74)
  • American Chemical Society (ACS)
  • Springer  (1)
Years
  • 1990-1994  (74)
Year
  • 1
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    Regulation of plasma membrane recycling by CFTR (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-04-24
    Description: The gene that encodes the cystic fibrosis transmembrane conductance regulator (CFTR) is defective in patients with cystic fibrosis. Although the protein product of the CFTR gene has been proposed to function as a chloride ion channel, certain aspects of its function remain unclear. The role of CFTR in the adenosine 3',5'-monophosphate (cAMP)-dependent regulation of plasma membrane recycling was examined. Adenosine 3',5'-monophosphate is known to regulate endocytosis and exocytosis in chloride-secreting epithelial cells that express CFTR. However, mutant epithelial cells derived from a patient with cystic fibrosis exhibited no cAMP-dependent regulation of endocytosis and exocytosis until they were transfected with complementary DNA encoding wild-type CFTR. Thus, CFTR is critical for cAMP-dependent regulation of membrane recycling in epithelial tissues, and this function of CFTR could explain in part the pleiotropic nature of cystic fibrosis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bradbury, N A -- Jilling, T -- Berta, G -- Sorscher, E J -- Bridges, R J -- Kirk, K L -- New York, N.Y. -- Science. 1992 Apr 24;256(5056):530-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology and Biophysics, University of Alabama, Birmingham 35294.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1373908" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cell Membrane/*physiology ; Chlorides/metabolism ; Colforsin/pharmacology ; Cyclic AMP/pharmacology ; Cystic Fibrosis/*physiopathology ; Cystic Fibrosis Transmembrane Conductance Regulator ; DNA/genetics ; Endocytosis/drug effects/physiology ; Epithelium/secretion ; Exocytosis/drug effects/physiology ; Gene Expression ; Horseradish Peroxidase/metabolism ; Humans ; Membrane Proteins/genetics/*physiology ; Molecular Sequence Data ; Pancreatic Neoplasms ; Transfection ; Tumor Cells, Cultured ; Wheat Germ Agglutinins/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    Repression of the insulin-like growth factor II gene by the Wilms tumor suppressor WT1 (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-07-31
    Description: The Wilms tumor suppressor gene wt1 encodes a zinc finger DNA binding protein, WT1, that functions as a transcriptional repressor. The fetal mitogen insulin-like growth factor II (IGF-II) is overexpressed in Wilms tumors and may have autocrine effects in tumor progression. The major fetal IGF-II promoter was defined in transient transfection assays as a region spanning from nucleotides -295 to +135, relative to the transcription start site. WT1 bound to multiple sites in this region and functioned as a potent repressor of IGF-II transcription in vivo. Maximal repression was dependent on the presence of WT1 binding sites on each side of the transcriptional initiation site. These findings provide a molecular basis for overexpression of IGF-II in Wilms tumors and suggest that WT1 negatively regulates blastemal cell proliferation by limiting the production of a fetal growth factor in the developing vertebrate kidney.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Drummond, I A -- Madden, S L -- Rohwer-Nutter, P -- Bell, G I -- Sukhatme, V P -- Rauscher, F J 3rd -- CA 10817/CA/NCI NIH HHS/ -- CA 47983/CA/NCI NIH HHS/ -- CA 52009/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1992 Jul 31;257(5070):674-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, University of Chicago, IL 60637.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1323141" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Binding Sites ; Blotting, Northern ; DNA/chemistry/metabolism ; DNA-Binding Proteins/*metabolism ; Deoxyribonuclease I/metabolism ; *Gene Expression Regulation, Neoplastic ; Genes, Wilms Tumor/*physiology ; Humans ; Insulin-Like Growth Factor II/*genetics ; Kidney/embryology/metabolism ; Mice ; Molecular Sequence Data ; Promoter Regions, Genetic ; Rats ; Sequence Homology, Nucleic Acid ; Transfection ; WT1 Proteins ; Wilms Tumor/genetics/metabolism ; Zinc Fingers
    Print ISSN: 0036-8075
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  • 3
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    The fms-like tyrosine kinase, a receptor for vascular endothelial growth factor (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-02-21
    Description: The fms-like tyrosine kinase (Flt) is a transmembrane receptor in the tyrosine kinase family. Expression of flt complementary DNA in COS cells conferred specific, high-affinity binding of vascular endothelial growth factor, also known as vascular permeability factor (VEGF-VPF), a factor that induces vascular permeability when injected in the guinea pig skin and stimulates endothelial cell proliferation. Expression of Flt in Xenopus laevis oocytes caused the oocytes to release calcium in response to VEGF-VPF. These findings show that flt encodes a receptor for VEGF-VPF.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉de Vries, C -- Escobedo, J A -- Ueno, H -- Houck, K -- Ferrara, N -- Williams, L T -- P01 HL-43821/HL/NHLBI NIH HHS/ -- R01 HL-32898/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1992 Feb 21;255(5047):989-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of California, San Francisco 94143.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1312256" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cloning, Molecular ; Cross-Linking Reagents ; Endothelial Growth Factors/*physiology ; Enzyme Activation ; Humans ; In Vitro Techniques ; Lymphokines/*physiology ; Proto-Oncogene Proteins/genetics/*physiology ; Receptors, Cell Surface/*genetics ; Signal Transduction ; Transfection ; Vascular Endothelial Growth Factor A ; Vascular Endothelial Growth Factor Receptor-1 ; Vascular Endothelial Growth Factors ; Xenopus laevis
    Print ISSN: 0036-8075
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  • 4
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    Acetylcholine receptor channel structure probed in cysteine-substitution mutants (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-10-09
    Description: In order to understand the structural bases of ion conduction, ion selectivity, and gating in the nicotinic acetylcholine receptor, mutagenesis and covalent modification were combined to identify the amino acid residues that line the channel. The side chains of alternate residues--Ser248, Leu250, Ser252, and Thr254--in M2, a membrane-spanning segment of the alpha subunit, are exposed in the closed channel. Thus alpha 248-254 probably forms a beta strand, and the gate is closer to the cytoplasmic end of the channel than any of these residues. On channel opening, Leu251 is also exposed. These results lead to a revised view of the closed and open channel structures.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Akabas, M H -- Stauffer, D A -- Xu, M -- Karlin, A -- NS07065/NS/NINDS NIH HHS/ -- NS07258/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1992 Oct 9;258(5080):307-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology, College of Physicians and Surgeons, Columbia University, New York, NY 10032.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1384130" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylcholine/metabolism/pharmacology ; Amino Acid Sequence ; Animals ; Cysteine/*chemistry ; Gene Expression ; Ion Channel Gating ; Ion Channels/*chemistry/physiology ; Mice ; Molecular Sequence Data ; Muscles/chemistry ; *Mutagenesis ; Oocytes/metabolism ; Receptors, Cholinergic/*chemistry/genetics ; Structure-Activity Relationship ; Sulfhydryl Reagents/pharmacology ; Thermodynamics ; Transfection ; Xenopus
    Print ISSN: 0036-8075
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  • 5
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    Targeted degradation of c-Fos, but not v-Fos, by a phosphorylation-dependent signal on c-Jun (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-12-18
    Description: The proto-oncogene products c-Fos and c-Jun heterodimerize through their leucine zippers to form the AP-1 transcription factor. The transcriptional activity of the heterodimer is regulated by signal-dependent phosphorylation and dephosphorylation events. The stability of c-Fos was found to also be controlled by intracellular signal transduction. In transient expression and in vitro degradation experiments, the stability of c-Fos was decreased when the protein was dimerized with phosphorylated c-Jun. c-Jun protein isolated from phorbol ester-induced cells did not target c-Fos for degradation, which suggests that c-Fos is transiently stabilized after stimulation of cell growth. v-Fos protein, the retroviral counterpart of c-Fos, was not susceptible to degradation targeted by c-Jun.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Papavassiliou, A G -- Treier, M -- Chavrier, C -- Bohmann, D -- New York, N.Y. -- Science. 1992 Dec 18;258(5090):1941-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉European Molecular Biology Laboratory, Differentiation Program, Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1470918" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Codon/genetics ; HeLa Cells ; Humans ; Macromolecular Substances ; Molecular Sequence Data ; Oncogene Proteins v-fos/genetics/*metabolism ; Phosphorylation ; Protein Biosynthesis ; Proto-Oncogene Proteins c-fos/genetics/*metabolism ; Proto-Oncogene Proteins c-jun/genetics/*metabolism ; Rabbits ; Recombinant Proteins/metabolism ; Reticulocytes/metabolism ; Tetradecanoylphorbol Acetate/pharmacology ; Transcription, Genetic ; Transfection
    Print ISSN: 0036-8075
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  • 6
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    The Autographa californica baculovirus genome: evidence for multiple replication origins (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-09-04
    Description: The Autographa californica multinucleocapsid nuclear polyhedrosis virus (AcMNPV), which is used for the overexpression of eukaryotic genes and is being engineered for possible use as a viral insecticide, has a circular, supercoiled genome of approximately 128 kilobases. Despite its widespread use, little is known about the mechanism by which AcMNPV replicates. Evidence is presented in this report that AcMNPV origins of DNA replication are repeated sequences each containing several closely related imperfect palindromes that are present in six regions distributed around the genome. Although AcMNPV infection-dependent plasmid replication was initiated by a single complete palindrome, the amount of replication was substantially increased in plasmids containing six or eight palindromes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pearson, M -- Bjornson, R -- Pearson, G -- Rohrmann, G -- AI21973/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1992 Sep 4;257(5075):1382-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Agricultural Chemistry, Oregon State University, Corvallis 97331.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1529337" target="_blank"〉PubMed〈/a〉
    Keywords: Baculoviridae/*genetics ; Base Sequence ; *DNA Replication ; DNA, Superhelical/chemistry/*genetics ; DNA, Viral/chemistry/*genetics ; Genes, Viral/*genetics ; Molecular Sequence Data ; Mutagenesis ; Nucleic Acid Hybridization ; Plasmids ; Repetitive Sequences, Nucleic Acid ; Transfection ; *Virus Replication
    Print ISSN: 0036-8075
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  • 7
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    Dual-target inhibition of HIV-1 in vitro by means of an adeno-associated virus antisense vector (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-12-07
    Description: An adeno-associated virus vector encoding an antisense RNA was used to transduce stable intracellular resistance to human immunodeficiency virus-1 (HIV-1) in human hemopoietic and non-hemopoietic cell lines. The antisense targets are present in all HIV-1 transcripts and include the TAR sequence, which is critical for transcription and virus replication, and the polyadenylation signal. Cell lines expressing antisense RNA showed up to 95 percent inhibition of gene expression directed by the HIV-1 long terminal repeat and greater than 99 percent reduction in infectious HIV-1 production, with no detectable cellular toxicity. Because of their efficient transcription and inability to recombine with HIV-1, adeno-associated virus vectors represent a promising form of anti-retroviral gene therapy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chatterjee, S -- Johnson, P R -- Wong, K K Jr -- New York, N.Y. -- Science. 1992 Nov 27;258(5087):1485-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Viral Diseases, National Institute of Allergy and Infectious Diseases (NIAID), National Institutes of Health, Rockville, MD 20852.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1359646" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; CD4-Positive T-Lymphocytes/microbiology ; Cell Line ; Chloramphenicol O-Acetyltransferase/genetics ; Dependovirus/*genetics ; Drug Resistance, Microbial/genetics ; Gene Products, tat/genetics ; Genetic Vectors/*genetics ; HIV Long Terminal Repeat/genetics ; HIV-1/*genetics/physiology ; Humans ; Molecular Sequence Data ; Neomycin/pharmacology ; RNA, Antisense/*genetics ; RNA, Messenger/genetics ; RNA, Viral/genetics ; Transfection ; Virus Replication/genetics ; tat Gene Products, Human Immunodeficiency Virus
    Print ISSN: 0036-8075
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  • 8
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    Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-04-17
    Description: Water rapidly crosses the plasma membrane of red blood cells (RBCs) and renal tubules through specialized channels. Although selective for water, the molecular structure of these channels is unknown. The CHIP28 protein is an abundant integral membrane protein in mammalian RBCs and renal proximal tubules and belongs to a family of membrane proteins with unknown functions. Oocytes from Xenopus laevis microinjected with in vitro-transcribed CHIP28 RNA exhibited increased osmotic water permeability; this was reversibly inhibited by mercuric chloride, a known inhibitor of water channels. Therefore it is likely that CHIP28 is a functional unit of membrane water channels.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Preston, G M -- Carroll, T P -- Guggino, W B -- Agre, P -- DK32753/DK/NIDDK NIH HHS/ -- HL33991/HL/NHLBI NIH HHS/ -- HL48268/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1992 Apr 17;256(5055):385-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, Johns Hopkins University School of Medicine, Baltimore, MD 21205.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1373524" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Aquaporin 1 ; *Aquaporins ; Cell Membrane Permeability ; Electric Conductivity ; Erythrocyte Membrane/*metabolism ; Immunoblotting ; Membrane Proteins/chemistry/genetics/*physiology ; Mercuric Chloride/pharmacology ; Molecular Structure ; Oocytes/*metabolism ; Osmolar Concentration ; RNA/genetics ; Thermodynamics ; Transfection ; Water/*metabolism ; Xenopus laevis
    Print ISSN: 0036-8075
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  • 9
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    Cytoplasmic domain heterogeneity and functions of IgG Fc receptors in B lymphocytes (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-06-26
    Description: B lymphocytes and macrophages express closely related immunoglobulin G (IgG) Fc receptors (Fc gamma RII) that differ only in the structures of their cytoplasmic domains. Because of cell type-specific alternative messenger RNA splicing, B-cell Fc gamma RII contains an insertion of 47 amino acids that participates in determining receptor function in these cells. Transfection of an Fc gamma RII-negative B-cell line with complementary DNA's encoding the two splice products and various receptor mutants indicated that the insertion was responsible for preventing both Fc gamma RII-mediated endocytosis and Fc gamma RII-mediated antigen presentation. The insertion was not required for Fc gamma RII to modulate surface immunoglobulin-triggered B-cell activation. Instead, regulation of activation involved a region of the cytoplasmic domain common to both the lymphocyte and macrophage receptor isoforms. In contrast, the insertion did contribute to the formation of caps in response to receptor cross-linking, consistent with suggestions that the lymphocyte but not macrophage form of the receptor can associate with the detergent-insoluble cytoskeleton.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Amigorena, S -- Bonnerot, C -- Drake, J R -- Choquet, D -- Hunziker, W -- Guillet, J G -- Webster, P -- Sautes, C -- Mellman, I -- Fridman, W H -- New York, N.Y. -- Science. 1992 Jun 26;256(5065):1808-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratoire d'Immunologie Cellulaire et Clinique, INSERM U 255, Institut Curie, Paris, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1535455" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Antigen-Antibody Complex/metabolism ; Antigen-Antibody Reactions/genetics/immunology ; Antigens, CD/genetics/*immunology ; Antigens, Differentiation/genetics/*immunology ; B-Lymphocytes/*immunology ; Calcium/metabolism ; *DNA-Binding Proteins ; Dose-Response Relationship, Immunologic ; Endocytosis/genetics/immunology ; Humans ; Immunohistochemistry ; Lymphocyte Activation/immunology ; Microscopy, Electron ; Molecular Sequence Data ; Receptors, Fc/genetics/*immunology ; Receptors, IgG ; Repressor Proteins/pharmacology ; Transcription Factors/pharmacology ; Transfection ; Viral Proteins ; Viral Regulatory and Accessory Proteins
    Print ISSN: 0036-8075
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  • 10
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    Molecular cloning of the interleukin-1 beta converting enzyme (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-04-03
    Description: Interleukin-1 beta (IL-1 beta) mediates a wide range of immune and inflammatory responses. The active cytokine is generated by proteolytic cleavage of an inactive precursor. A complementary DNA encoding a protease that carries out this cleavage has been cloned. Recombinant expression in COS-7 cells enabled the cells to process precursor IL-1 beta to the mature form. Sequence analysis indicated that the enzyme itself may undergo proteolytic processing. The gene encoding the protease was mapped to chromosomal band 11q23, a site frequently involved in rearrangement in human cancers.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cerretti, D P -- Kozlosky, C J -- Mosley, B -- Nelson, N -- Van Ness, K -- Greenstreet, T A -- March, C J -- Kronheim, S R -- Druck, T -- Cannizzaro, L A -- New York, N.Y. -- Science. 1992 Apr 3;256(5053):97-100.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Immunex Corporation, Seattle, WA 98101.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1373520" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Caspase 1 ; Cell Line ; Chromosome Banding ; *Chromosomes, Human, Pair 11 ; Cloning, Molecular ; Enzyme Precursors/biosynthesis/*genetics/isolation & purification ; Humans ; Metalloendopeptidases/biosynthesis/*genetics/isolation & purification ; Molecular Sequence Data ; Neutrophils/enzymology ; Oligodeoxyribonucleotides ; Poly A/genetics/isolation & purification ; Polymerase Chain Reaction/methods ; RNA/genetics/isolation & purification ; RNA, Messenger/genetics ; Recombinant Proteins/biosynthesis/isolation & purification ; Transfection
    Print ISSN: 0036-8075
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  • 11
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    Regulatory elements that control the lineage-specific expression of myoD (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-05-04
    Description: The molecular basis of skeletal muscle lineage determination was investigated by analyzing DNA control elements that regulate the myogenic determination gene myoD. A distal enhancer was identified that positively regulates expression of the human myoD gene. The myoD enhancer and promoter were active in myogenic and several nonmyogenic cell lines. In transgenic mouse embryos, however, the myoD enhancer and promoter together directed expression of a lacZ transgene specifically to the skeletal muscle lineage. These data suggest that during development myoD is regulated by mechanisms that restrict accessibility of myoD control elements to positive trans-acting factors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Goldhamer, D J -- Faerman, A -- Shani, M -- Emerson, C P Jr -- CA-06927/CA/NCI NIH HHS/ -- HD-07796/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 1992 Apr 24;256(5056):538-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute for Cancer Research, Fox Chase Cancer Center, Philadelphia, PA 19111.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1315077" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Differentiation ; Cell Line ; Chloramphenicol O-Acetyltransferase/genetics ; Cloning, Molecular ; Enhancer Elements, Genetic ; *Gene Expression Regulation ; Humans ; Mice ; Mice, Transgenic ; Muscle Proteins/*genetics ; Muscles/embryology/metabolism ; MyoD Protein ; Promoter Regions, Genetic ; Transcription, Genetic ; Transfection ; Tumor Cells, Cultured ; beta-Galactosidase/genetics
    Print ISSN: 0036-8075
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  • 12
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    Interaction cloning: identification of a helix-loop-helix zipper protein that interacts with c-Fos (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-05-15
    Description: A facile method for isolating genes that encode interacting proteins has been developed with a polypeptide probe that contains an amino-terminal extension with recognition sites for a monoclonal antibody, a specific endopeptidase, and a site-specific protein kinase. This probe, containing the basic region-leucine zipper dimerization motif of c-Fos, was used to screen a complementary DNA library. A complementary DNA that encoded a member of the basic-helix-loop-helix-zipper (bHLH-Zip) family of proteins was isolated. The complementary DNA-encoded polypeptide FIP (Fos interacting protein) bound to oligonucleotide probes that contained DNA binding motifs for other HLH proteins. When cotransfected with c-Fos, FIP stimulated transcription of an AP-1-responsive promoter.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Blanar, M A -- Rutter, W J -- DK-21344/DK/NIDDK NIH HHS/ -- DK-41822/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1992 May 15;256(5059):1014-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Hormone Research Institute, University of California, San Francisco 94143.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1589769" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; *Cloning, Molecular ; DNA/isolation & purification ; DNA-Binding Proteins/chemistry/genetics/*metabolism ; *Genes, fos/genetics ; HeLa Cells ; Humans ; Leucine Zippers/*genetics ; Macromolecular Substances ; Molecular Sequence Data ; Oligonucleotide Probes/chemistry/metabolism ; Protein Conformation ; Proto-Oncogene Proteins c-fos/chemistry/metabolism ; Proto-Oncogene Proteins c-jun/chemistry/metabolism ; Sequence Homology, Nucleic Acid ; Transfection
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  • 13
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    A human gene responsible for Zellweger syndrome that affects peroxisome assembly (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-02-28
    Description: The primary defect arising from Zellweger syndrome appears to be linked to impaired assembly of peroxisomes. A human complementary DNA has been cloned that complements the disease's symptoms (including defective peroxisome assembly) in fibroblasts from a patient with Zellweger syndrome. The cause of the syndrome in this patient was a point mutation that resulted in the premature termination of peroxisome assembly factor-1. The homozygous patient apparently inherited the mutation from her parents, each of whom was heterozygous for that mutation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shimozawa, N -- Tsukamoto, T -- Suzuki, Y -- Orii, T -- Shirayoshi, Y -- Mori, T -- Fujiki, Y -- New York, N.Y. -- Science. 1992 Feb 28;255(5048):1132-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pediatrics, Gifu University School of Medicine, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1546315" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Cricetinae ; DNA Mutational Analysis ; Genes ; Genetic Complementation Test ; Humans ; Membrane Proteins/*genetics ; Microbodies/*ultrastructure ; Molecular Sequence Data ; Oligodeoxyribonucleotides/chemistry ; Pedigree ; Polymerase Chain Reaction ; Transfection ; Zellweger Syndrome/*genetics
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  • 14
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    Human and Drosophila homeodomain proteins that enhance the DNA-binding activity of serum response factor (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-08-21
    Description: Cells with distinct developmental histories can respond differentially to identical signals, suggesting that signals are interpreted in a fashion that reflects a cell's identity. How this might occur is suggested by the observation that proteins of the homeodomain family, including a newly identified human protein, enhance the DNA-binding activity of serum response factor, a protein required for the induction of genes by growth and differentiation factors. Interaction with proteins of the serum response factor family may allow homeodomain proteins to specify the transcriptional response to inductive signals. Moreover, because the ability to enhance the binding of serum response factor to DNA residues within the homeodomain but is independent of homeodomain DNA-binding activity, this additional activity of the homeodomain may account for some of specificity of action of homeodomain proteins in development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Grueneberg, D A -- Natesan, S -- Alexandre, C -- Gilman, M Z -- CA08968/CA/NCI NIH HHS/ -- CA45642/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1992 Aug 21;257(5073):1089-95.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cold Spring Harbor Laboratory, NY 11724.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1509260" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Binding Sites ; DNA/genetics/*metabolism ; DNA-Binding Proteins/chemistry/genetics/*metabolism/*pharmacology ; Drosophila/genetics ; *Drosophila Proteins ; Fungal Proteins/chemistry/pharmacology ; *Homeodomain Proteins ; Humans ; Minichromosome Maintenance 1 Protein ; Molecular Sequence Data ; Nuclear Proteins/*metabolism ; Saccharomyces cerevisiae/genetics ; Serum Response Factor ; Transcription Factors/chemistry/*metabolism/pharmacology ; Transfection
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 15
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    NF-kappa B subunit regulation in nontransformed CD4+ T lymphocytes (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-06-05
    Description: Regulation of interleukin-2 (IL-2) gene expression by the p50 and p65 subunits of the DNA binding protein NF-kappa B was studied in nontransformed CD4+ T lymphocyte clones. A homodimeric complex of the NF-kappa B p50 subunit was found in resting T cells. The amount of p50-p50 complex decreased after full antigenic stimulation, whereas the amount of the NF-kappa B p50-p65 heterodimer was increased. Increased expression of the IL-2 gene and activity of the IL-2 kappa B DNA binding site correlated with a decrease in the p50-p50 complex. Overexpression of p50 repressed IL-2 promoter expression. The switch from p50-p50 to p50-p65 complexes depended on a protein that caused sequestration of the p50-p50 complex in the nucleus.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kang, S M -- Tran, A C -- Grilli, M -- Lenardo, M J -- New York, N.Y. -- Science. 1992 Jun 5;256(5062):1452-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Immunology, National Institute for Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1604322" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD4/*immunology ; Base Sequence ; Binding Sites ; Cell Line ; Cell Nucleus/physiology ; Chloramphenicol O-Acetyltransferase/genetics/metabolism ; Clone Cells ; Columbidae ; DNA/genetics ; *Gene Expression Regulation ; Interleukin-2/*genetics ; Macromolecular Substances ; Mice ; Molecular Sequence Data ; NF-kappa B/*metabolism ; Oligonucleotide Probes ; Promoter Regions, Genetic ; RNA, Messenger/metabolism ; Recombinant Fusion Proteins/metabolism ; T-Lymphocyte Subsets/*immunology ; Transfection ; Tumor Necrosis Factor-alpha/pharmacology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 16
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    Structure and functional expression of an omega-conotoxin-sensitive human N-type calcium channel (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-07-17
    Description: N-type calcium channels are omega-conotoxin (omega-CgTx)-sensitive, voltage-dependent ion channels involved in the control of neurotransmitter release from neurons. Multiple subtypes of voltage-dependent calcium channel complexes exist, and it is the alpha 1 subunit of the complex that forms the pore through which calcium enters the cell. The primary structures of human neuronal calcium channel alpha 1B subunits were deduced by the characterization of overlapping complementary DNAs. Two forms (alpha 1B-1 and alpha 1B-2) were identified in human neuroblastoma (IMR32) cells and in the central nervous system, but not in skeletal muscle or aorta tissues. The alpha 1B-1 subunit directs the recombinant expression of N-type calcium channel activity when it is transiently co-expressed with human neuronal beta 2 and alpha 2b subunits in mammalian HEK293 cells. The recombinant channel was irreversibly blocked by omega-CgTx but was insensitive to dihydropyridines. The alpha 1B-1 alpha 2b beta 2-transfected cells displayed a single class of saturable, high-affinity (dissociation constant = 55 pM) omega-CgTx binding sites. Co-expression of the beta 2 subunit was necessary for N-type channel activity, whereas the alpha 2b subunit appeared to modulate the expression of the channel. The heterogeneity of alpha 1B subunits, along with the heterogeneity of alpha 2 and beta subunits, is consistent with multiple, biophysically distinct N-type calcium channels.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Williams, M E -- Brust, P F -- Feldman, D H -- Patthi, S -- Simerson, S -- Maroufi, A -- McCue, A F -- Velicelebi, G -- Ellis, S B -- Harpold, M M -- New York, N.Y. -- Science. 1992 Jul 17;257(5068):389-95.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉SIBIA, Inc., La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1321501" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Calcium/metabolism ; Calcium Channels/*drug effects/*genetics/*metabolism ; Cell Line ; Female ; Humans ; Male ; Membrane Potentials ; Molecular Sequence Data ; Neuroblastoma/metabolism ; Peptides, Cyclic/*pharmacology ; Sequence Alignment ; Sequence Homology, Nucleic Acid ; Transfection ; omega-Conotoxin GVIA
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  • 17
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    Oncogenic forms of p53 inhibit p53-regulated gene expression (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-05-08
    Description: Mutant forms of the gene encoding the tumor suppressor p53 are found in numerous human malignancies, but the physiologic function of p53 and the effects of mutations on this function are unknown. The p53 protein binds DNA in a sequence-specific manner and thus may regulate gene transcription. Cotransfection experiments showed that wild-type p53 activated the expression of genes adjacent to a p53 DNA binding site. The level of activation correlated with DNA binding in vitro. Oncogenic forms of p53 lost this activity. Moreover, all mutants inhibited the activity of coexpressed wild-type p53, providing a basis for the selection of such mutants during tumorigenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kern, S E -- Pietenpol, J A -- Thiagalingam, S -- Seymour, A -- Kinzler, K W -- Vogelstein, B -- CA06973/CA/NCI NIH HHS/ -- CA09243/CA/NCI NIH HHS/ -- CA35494/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1992 May 8;256(5058):827-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Johns Hopkins University School of Medicine, Baltimore, MD 21231.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1589764" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cell Line ; Chloramphenicol O-Acetyltransferase/genetics/metabolism ; DNA-Binding Proteins/*genetics/*metabolism ; Exons ; *Gene Expression Regulation, Neoplastic ; *Genes, p53 ; Genetic Vectors ; Humans ; Molecular Sequence Data ; Oligodeoxyribonucleotides ; Polymerase Chain Reaction/methods ; Recombinant Fusion Proteins/metabolism ; Repetitive Sequences, Nucleic Acid ; Saccharomyces cerevisiae/genetics/growth & development ; *Transcription, Genetic ; Transfection ; Tumor Suppressor Protein p53/*genetics/*metabolism ; beta-Galactosidase/genetics/metabolism
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  • 18
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    Calcium-dependent transmitter secretion reconstituted in Xenopus oocytes: requirement for synaptophysin (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-07-31
    Description: Calcium-dependent glutamate secretion was reconstituted in Xenopus oocytes by injecting the oocyte with total rat cerebellar messenger RNA (mRNA). Co-injection of total mRNA with antisense oligonucleotides to synaptophysin message decreased the expression of synaptophysin in the oocyte and reduced the calcium-dependent secretion. A similar effect on secretion was observed for oocytes injected with total mRNA together with an antibody to rat synaptophysin. These results indicate that synaptophysin is necessary for transmitter secretion and that the oocyte expression system may be useful for dissecting the molecular events associated with the secretory process.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Alder, J -- Lu, B -- Valtorta, F -- Greengard, P -- Poo, M M -- MH 39327/MH/NIMH NIH HHS/ -- NS 22764/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1992 Jul 31;257(5070):657-61.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, Columbia University, New York, NY 10027.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1353905" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Blotting, Western ; Calcimycin/pharmacology ; Calcium/*pharmacology ; Cerebellum/chemistry ; Fluorescent Antibody Technique ; Gene Expression ; Glutamates/*secretion ; Glutamic Acid ; Kinetics ; Liver/chemistry ; Microscopy, Immunoelectron ; Molecular Sequence Data ; Oligonucleotides, Antisense/pharmacology ; Oocytes/*physiology ; RNA, Messenger/genetics ; Rats ; Synaptophysin/genetics/*physiology ; Transfection ; Xenopus
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  • 19
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    Gz-mediated hormonal inhibition of cyclic AMP accumulation (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-01-17
    Description: Hormones inhibit synthesis of adenosine 3',5'-monophosphate (cAMP) in most cells via receptors coupled to pertussis toxin (PTX)-sensitive guanine nucleotide-binding (G) proteins. Mutationally activated alpha subunits of Gi2 (alpha i2) constitutively inhibit cAMP accumulation when transfected into cells. Cells have now been transfected with mutant alpha subunits of four other G proteins--Gz, a PTX-insensitive G protein of unknown function, and Gi1, Gi3, and G(o), which are PTX-sensitive. Mutant alpha z, alpha i1, and alpha i3 inhibited cAMP accumulation but alpha o did not. Moreover, expression of wild-type alpha z produced cells in which PTX did not block hormonal inhibition of cAMP accumulation. Thus, Gz can trigger an effector pathway in response to hormone receptors that ordinarily interact with PTX-sensitive Gi proteins.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wong, Y H -- Conklin, B R -- Bourne, H R -- New York, N.Y. -- Science. 1992 Jan 17;255(5042):339-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of California, San Francisco 94143.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1347957" target="_blank"〉PubMed〈/a〉
    Keywords: Adrenergic alpha-Agonists/pharmacology ; Animals ; Brimonidine Tartrate ; Chorionic Gonadotropin/pharmacology ; Colforsin/pharmacology ; Cyclic AMP/*biosynthesis ; Dinoprostone/pharmacology ; Dopamine/pharmacology ; GTP-Binding Proteins/*physiology ; Gene Expression Regulation/*physiology ; Hormones/*physiology ; In Vitro Techniques ; Lysophospholipids/pharmacology ; Pertussis Toxin ; Quinoxalines/pharmacology ; Rats ; Signal Transduction/physiology ; Transfection ; Virulence Factors, Bordetella/pharmacology
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  • 20
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    Participation of non-zinc finger residues in DNA binding by two nuclear orphan receptors (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-04-03
    Description: Steroid-thyroid hormone receptors typically bind as dimers to DNA sequences that contain repeated elements termed half-sites. NGFI-B, an early response protein and orphan member of this receptor superfamily, binds to a DNA sequence that contains only one half-site (5'-AAAGGTCA-3'). A domain separate from the NGFI-B zinc fingers, termed the A box, was identified and is required for recognition of the two adenine-thymidine (A-T) base pairs at the 5' end of the NGFI-B DNA binding element. In addition, a domain downstream of the zinc fingers of the orphan receptor H-2 region II binding protein, termed the T box, determined binding to tandem repeats of the estrogen receptor half-site (5'-AGGTCA-3').〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wilson, T E -- Paulsen, R E -- Padgett, K A -- Milbrandt, J -- NS01018/NS/NINDS NIH HHS/ -- P01 CA49712/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1992 Apr 3;256(5053):107-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Washington University School of Medicine, St. Louis, MO 63110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1314418" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Binding Sites ; CHO Cells ; Cell Nucleus/*physiology ; Cricetinae ; DNA/*metabolism ; DNA-Binding Proteins/genetics/*metabolism ; Kinetics ; Mice ; Molecular Sequence Data ; Nuclear Receptor Subfamily 4, Group A, Member 1 ; Oligodeoxyribonucleotides/metabolism ; Polymerase Chain Reaction ; Receptors, Cell Surface/*metabolism ; Receptors, Cytoplasmic and Nuclear ; Receptors, Steroid ; Recombinant Fusion Proteins/metabolism ; Sequence Homology, Nucleic Acid ; Substrate Specificity ; Transcription Factors/genetics/*metabolism ; Transfection ; Zinc Fingers/genetics
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    High-efficiency expression and solubilization of functional T cell antigen receptor heterodimers (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-05-29
    Description: The T cell receptor (TCR) zeta chain was attached to the TCR alpha and beta extracellular domains to induce efficient expression of alpha beta heterodimers that can recognize complexes of antigen with major histocompatibility complex (MHC) molecules. Chimeric constructs expressed in RBL-2H3 cells were efficiently transported to the cell surface uniquely as disulfide-linked heterodimers. Transfectants were activated by specific antigen-MHC complexes, which demonstrated that the expressed alpha beta was functional and that CD3 was not required for antigen-MHC binding. Constructs with thrombin cleavage sites were efficiently cleaved to soluble disulfide-linked heterodimers. Thus, attachment of TCR zeta domains and protease cleavage sites to TCR alpha and beta induces expression of demonstrably functional heterodimers that can be solubilized.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Engel, I -- Ottenhoff, T H -- Klausner, R D -- New York, N.Y. -- Science. 1992 May 29;256(5061):1318-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1598575" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Line ; Cell Membrane/immunology ; Disulfides ; Flow Cytometry ; Histocompatibility Antigens/metabolism ; Kinetics ; Macromolecular Substances ; Molecular Sequence Data ; Oligodeoxyribonucleotides ; Polymerase Chain Reaction ; Receptors, Antigen, T-Cell/genetics/isolation & purification/*metabolism ; Solubility ; Transfection
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  • 22
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    Mutation of the POU-specific domain of Pit-1 and hypopituitarism without pituitary hypoplasia (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-08-21
    Description: A point mutation in the POU-specific portion of the human gene that encodes the tissue-specific POU-domain transcription factor, Pit-1, results in hypopituitarism, with deficiencies of growth hormone, prolactin, and thyroid-stimulating hormone. In two unrelated Dutch families, a mutation in Pit-1 that altered an alanine in the first putative alpha helix of the POU-specific domain to proline was observed. This mutation generated a protein capable of binding to DNA response elements but unable to effectively activate its known target genes, growth hormone and prolactin. The phenotype of the affected individuals suggests that the mutant Pit-1 protein is competent to initiate other programs of gene activation required for normal proliferation of somatotrope, lactotrope, and thyrotrope cell types. Thus, a mutation in the POU-specific domain of Pit-1 has a selective effect on a subset of Pit-1 target genes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pfaffle, R W -- DiMattia, G E -- Parks, J S -- Brown, M R -- Wit, J M -- Jansen, M -- Van der Nat, H -- Van den Brande, J L -- Rosenfeld, M G -- Ingraham, H A -- HD24960/HD/NICHD NIH HHS/ -- HD2697/HD/NICHD NIH HHS/ -- NIDDK 18477/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1992 Aug 21;257(5073):1118-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pediatrics, Emory University School of Medicine, Atlanta, GA 30322.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1509263" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Blotting, Northern ; DNA/chemistry/metabolism ; DNA-Binding Proteins/*genetics/metabolism ; Growth Hormone/deficiency ; Humans ; Hypopituitarism/*genetics/pathology ; Mice ; Molecular Sequence Data ; *Mutation ; Nucleic Acid Hybridization ; Pituitary Gland, Anterior/*pathology ; Pituitary Hormones/*deficiency ; Polymerase Chain Reaction ; Prolactin/deficiency ; Rats ; Sequence Homology, Nucleic Acid ; Thyrotropin/deficiency ; Transcription Factor Pit-1 ; Transcription Factors/*genetics/metabolism ; Transfection
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  • 23
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    Control by asparagine residues of calcium permeability and magnesium blockade in the NMDA receptor (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-09-04
    Description: The N-methyl-D-aspartate (NMDA) receptor forms a cation-selective channel with a high calcium permeability and sensitivity to channel block by extracellular magnesium. These properties, which are believed to be important for the induction of long-term changes in synaptic strength, are imparted by asparagine residues in a putative channel-forming segment of the protein, transmembrane 2 (TM2). In the NR1 subunit, replacement of this asparagine by a glutamine residue decreases calcium permeability of the channel and slightly reduces magnesium block. The same substitution in NR2 subunits strongly reduces magnesium block and increases the magnesium permeability but barely affects calcium permeability. These asparagines are in a position homologous to the site in the TM2 region (Q/R site) of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors that is occupied by either glutamine (Q) or arginine (R) and that controls divalent cation permeability of the AMPA receptor channel. Hence AMPA and NMDA receptor channels contain common structural motifs in their TM2 segments that are responsible for some of their ion selectivity and conductance properties.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Burnashev, N -- Schoepfer, R -- Monyer, H -- Ruppersberg, J P -- Gunther, W -- Seeburg, P H -- Sakmann, B -- New York, N.Y. -- Science. 1992 Sep 4;257(5075):1415-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Abteilung Zellphysiologie, Max-Planck-Institut fur Medizinische Forschung, Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1382314" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Asparagine/*chemistry ; Binding Sites ; Calcium/*metabolism/pharmacology ; Cell Line ; Electric Conductivity ; Glutamates/pharmacology ; Glutamic Acid ; Ion Channels/chemistry/*physiology ; Magnesium/metabolism/*pharmacology ; Mice ; Molecular Sequence Data ; Mutagenesis ; Oocytes/metabolism ; Permeability ; Rats ; Receptors, N-Methyl-D-Aspartate/chemistry/genetics/*physiology ; Structure-Activity Relationship ; Transfection ; Xenopus
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    Potentially amyloidogenic, carboxyl-terminal derivatives of the amyloid protein precursor (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-02-07
    Description: The 39- to 43-amino acid amyloid beta protein (beta AP), which is deposited as amyloid in Alzheimer's disease, is encoded as an internal peptide that begins 99 residues from the carboxyl terminus of a 695- to 770-amino acid glycoprotein referred to as the amyloid beta protein precursor (beta APP). To clarify the processing that produces amyloid, carboxyl-terminal derivatives of the beta APP were analyzed. This analysis showed that the beta APP is normally processed into a complex set of 8- to 12-kilodalton carboxyl-terminal derivatives. The two largest derivatives in human brain have the entire beta AP at or near their amino terminus and are likely to be intermediates in the pathway leading to amyloid deposition.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Estus, S -- Golde, T E -- Kunishita, T -- Blades, D -- Lowery, D -- Eisen, M -- Usiak, M -- Qu, X M -- Tabira, T -- Greenberg, B D -- AG06656/AG/NIA NIH HHS/ -- AG08012/AG/NIA NIH HHS/ -- AG08992/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 1992 Feb 7;255(5045):726-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Neuropathology, Case Western Reserve University, Cleveland, OH 44106.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1738846" target="_blank"〉PubMed〈/a〉
    Keywords: Amyloid/*biosynthesis ; Amyloid beta-Protein Precursor/chemistry/genetics/*metabolism ; Cell Line ; Cell Membrane/chemistry ; Cerebral Cortex/chemistry ; Glycosylation ; Humans ; Immunoblotting ; Immunosorbent Techniques ; Molecular Weight ; Peptide Fragments/chemistry/isolation & purification/*metabolism ; Transfection
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    Cloning of a delta opioid receptor by functional expression (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-12-28
    Description: Opiate drugs have potent analgesic and addictive properties. These drugs interact with receptors that also mediate the response to endogenous opioid peptide ligands. However, the receptors for opioids have eluded definitive molecular characterization. By transient expression in COS cells and screening with an iodinated analog of the opioid peptide enkephalin, a complementary DNA clone encoding a functional delta opioid receptor has been identified. The sequence shows homology to G protein-coupled receptors, in particular the receptors for somatostatin, angiotensin, and interleukin-8.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Evans, C J -- Keith, D E Jr -- Morrison, H -- Magendzo, K -- Edwards, R H -- DA05010/DA/NIDA NIH HHS/ -- P50 DA005010/DA/NIDA NIH HHS/ -- New York, N.Y. -- Science. 1992 Dec 18;258(5090):1952-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Psychiatry, University of California, School of Medicine, Los Angeles 90024-1759.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1335167" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding, Competitive ; Blotting, Northern ; Blotting, Southern ; Cell Line ; Cyclic AMP/metabolism ; Diprenorphine/metabolism ; Enkephalin, D-Penicillamine (2,5)- ; Enkephalins/pharmacology ; Etorphine/pharmacology ; Gene Expression ; Humans ; Kinetics ; Models, Structural ; Molecular Sequence Data ; Naloxone/pharmacology ; Narcotics/pharmacology ; Protein Structure, Secondary ; Receptors, Opioid, delta/chemistry/*genetics/*metabolism ; Sequence Homology, Amino Acid ; Transfection ; Tumor Cells, Cultured
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    Gene therapy for CF advances (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-01-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Marx, J -- New York, N.Y. -- Science. 1992 Jan 17;255(5042):289.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1549773" target="_blank"〉PubMed〈/a〉
    Keywords: Adenoviridae/genetics ; Animals ; Cystic Fibrosis/*therapy ; Genetic Therapy/*methods ; Genetic Vectors ; Rats ; Transfection
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  • 27
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    Thermal stability comparison of purified empty and peptide-filled forms of a class I MHC molecule (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-12-04
    Description: A secreted form of a class I major histocompatibility complex (MHC) molecule was denatured and renatured in vitro in the absence of peptide. The resulting empty class I heterodimer was immunologically reactive and structurally similar to a heterodimer renatured in the presence of an appropriate restricted peptide. Thermal stability profiles indicated that the two forms of heterodimer differed in their resistance to denaturation by heat but that a significant portion of the empty class I heterodimers had a native conformation at physiological temperatures. Free energies calculated from these data gave a direct measure of the stabilization of the class I MHC molecule that resulted from peptide binding.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fahnestock, M L -- Tamir, I -- Narhi, L -- Bjorkman, P J -- AI28931/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1992 Dec 4;258(5088):1658-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biology, California Institute of Technology, Pasadena 91125.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1360705" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; CHO Cells ; Circular Dichroism ; Cricetinae ; Drug Stability ; Enzyme-Linked Immunosorbent Assay ; Glutamate-Ammonia Ligase/genetics/metabolism ; Histocompatibility Antigens Class I/*chemistry/genetics ; Hot Temperature ; Humans ; Macromolecular Substances ; *Protein Conformation ; Protein Folding ; Thermodynamics ; Transfection
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  • 28
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    Calmodulin trapping by calcium-calmodulin-dependent protein kinase (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-05-22
    Description: Multifunctional calcium-calmodulin-dependent protein kinase (CaM kinase) transduces transient elevations in intracellular calcium into changes in the phosphorylation state and activity of target proteins. By fluorescence emission anisotropy, the affinity of CaM kinase for dansylated calmodulin was measured and found to increase 1000 times after autophosphorylation of the threonine at position 286 of the protein. Autophosphorylation markedly slowed the release of bound calcium-calmodulin; the release time increased from less than a second to several hundred seconds. In essence, calmodulin is trapped by autophosphorylation. The shift in affinity does not occur in a site-directed mutant in which threonine at position 286 has been replaced by a non-phosphorylatable amino acid. These experiments demonstrate the existence of a new state in which calmodulin is bound to CaM kinase even though the concentration of calcium is basal. Calmodulin trapping provides for molecular potentiation of calcium transients and may enable detection of their frequency.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Meyer, T -- Hanson, P I -- Stryer, L -- Schulman, H -- GM 40600/GM/NIGMS NIH HHS/ -- GM24032/GM/NIGMS NIH HHS/ -- MH45324/MH/NIMH NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1992 May 22;256(5060):1199-202.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Stanford University School of Medicine, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1317063" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Binding, Competitive ; Calcium/pharmacology ; Calcium-Calmodulin-Dependent Protein Kinases ; Calmodulin/*metabolism ; Cell Line ; Egtazic Acid/pharmacology ; Kinetics ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Phosphorylation ; Protein Binding ; Protein Kinases/genetics/*metabolism ; Recombinant Proteins/metabolism ; Spectrometry, Fluorescence ; Threonine ; Time Factors ; Transfection
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    A functional connection between the pores of distantly related ion channels as revealed by mutant K+ channels (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-11-13
    Description: The overall sequence similarity between the voltage-activated K+ channels and cyclic nucleotide-gated ion channels from retinal and olfactory neurons suggests that they arose from a common ancestor. On the basis of sequence comparisons, mutations were introduced into the pore of a voltage-activated K+ channel. These mutations confer the essential features of ion conduction in the cyclic nucleotide-gated ion channels; the mutant K+ channels display little selectivity among monovalent cations and are blocked by divalent cations. The property of K+ selectivity is related to the presence of two amino acids that are absent from the pore-forming region of the cyclic nucleotide-gated channels. These data demonstrate that very small differences in the primary structure of an ion channel can account for extreme functional diversity, and they suggest a possible connection between the pore-forming regions of K+, Ca2+, and cyclic nucleotide-gated ion channels.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Heginbotham, L -- Abramson, T -- MacKinnon, R -- GM43949/GM/NIGMS NIH HHS/ -- GM47400/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1992 Nov 13;258(5085):1152-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1279807" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Calcium/pharmacology ; Cattle ; Cyclic AMP/pharmacology ; Cyclic GMP/pharmacology ; Drosophila ; Electric Conductivity ; Ion Channel Gating/drug effects ; Ion Channels/drug effects/*physiology ; Magnesium/pharmacology ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Oocytes/physiology ; Plants ; Potassium Channels/chemistry/*genetics/*physiology ; Retina/ultrastructure ; Transfection ; Xenopus laevis
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  • 30
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    Malignant transformation by a mutant of the IFN-inducible dsRNA-dependent protein kinase (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-09-18
    Description: The double-stranded RNA-dependent protein kinase (dsRNA-PK) is thought to be a key mediator of the antiviral and antiproliferative effects of interferons (IFNs). Studies examining the physiological function of the kinase suggest that it participates in cell growth and differentiation by regulating protein synthesis. Autophosphorylation and consequent activation of dsRNA-PK in vitro and in vivo result in phosphorylation of the alpha subunit of eukaryotic initiation factor-2 (eIF-2) and inhibition of protein synthesis. Expression of a functionally defective mutant of human dsRNA-PK in NIH 3T3 cells resulted in malignant transformation, suggesting that dsRNA-PK may function as a suppressor of cell proliferation and tumorigenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Koromilas, A E -- Roy, S -- Barber, G N -- Katze, M G -- Sonenberg, N -- AI22646/AI/NIAID NIH HHS/ -- RR00166/RR/NCRR NIH HHS/ -- New York, N.Y. -- Science. 1992 Sep 18;257(5077):1685-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, Faculty of Medicine, McGill University, Montreal, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1382315" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Binding Sites ; Cell Division ; Cell Line ; *Cell Transformation, Neoplastic ; Cloning, Molecular ; DNA/genetics ; Enzyme Induction ; Gene Expression ; Humans ; Immunoblotting ; Interferons/*pharmacology ; Mice ; Molecular Sequence Data ; *Mutation ; Phosphorylation ; Protein Kinases/chemistry/*genetics/physiology ; Transfection ; eIF-2 Kinase
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    Implication of GAP in Ras-dependent transactivation of a polyoma enhancer sequence (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-05-08
    Description: Controversy exists as to whether the interaction of a guanosine triphosphatase activating protein (GAP) with Ras proteins functions both to initiate and to terminate Ras-dependent signaling events or only to terminate them. GAP-C, a carboxyl-terminal fragment of GAP that is sufficient to stimulate GTPase activity, inhibited the stimulation of transcription produced by some oncoproteins (v-Src, polyoma middle T, wild-type Ras, and oncogenic Ras) but not that produced by v-Mos. Wild-type GAP did not affect transcription induced by oncogenic Ras but reversed the inhibitory effect of GAP-C on transcription induced by oncogenic Ras. These results indicate that GAP is a negative regulator of wild-type Ras and elicits a downstream signal by interacting with Ras-GTP (guanosine triphosphate).〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schweighoffer, F -- Barlat, I -- Chevallier-Multon, M C -- Tocque, B -- New York, N.Y. -- Science. 1992 May 8;256(5058):825-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Rhone-Poulenc Rorer, Centre de Recherche de Vitry-Alfortville, Vitry Sur Seine.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1317056" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Animals ; Antigens, Polyomavirus Transforming/genetics ; CHO Cells ; *Cell Cycle Proteins ; *Cell Transformation, Neoplastic ; Chloramphenicol O-Acetyltransferase/genetics/metabolism ; Cricetinae ; *Enhancer Elements, Genetic ; Fungal Proteins/genetics/metabolism ; GTPase-Activating Proteins ; *Genes, ras ; Humans ; Mice ; Oncogene Proteins v-mos ; Oncogenes ; Polyomavirus/*genetics ; Promoter Regions, Genetic ; Protein-Tyrosine Kinases/genetics ; Proteins/*metabolism ; Retroviridae Proteins, Oncogenic/genetics ; Signal Transduction ; Simian virus 40/genetics ; Transcription, Genetic ; *Transcriptional Activation ; Transfection ; ras GTPase-Activating Proteins ; *ras-GRF1
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    Brain tumor treatment: significant contributions (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-12-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Blaese, R M -- Culver, K W -- Ishii, H -- Oldfield, E H -- Ram, Z -- Wallbridge, S -- New York, N.Y. -- Science. 1992 Dec 18;258(5090):1960.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1470923" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain Neoplasms/*therapy ; *Genetic Therapy ; Glioma ; Mice ; Retroviridae/genetics ; Thymidine Kinase/genetics ; Transfection ; Tumor Cells, Cultured ; beta-Galactosidase/genetics/metabolism
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    Initiation of deregulated growth of multipotent progenitor cells by bcr-abl in vitro (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-05-08
    Description: Expression of the bcr-abl oncogene in multipotent progenitor cells (MPPCs) is implicated as a key event in the development of chronic myelogenous leukemia. Bone marrow enriched for MPPCs was infected with a retrovirus that carried bcr-abl. The mixed-lineage colonies that resulted were responsive to growth factors and could differentiate. These cells later became growth factor-independent but, when injected into severe combined immunodeficient mice, were not leukemogenic. Thus, the presence of bcr-abl alone does not cause growth factor independence, although it initiates a stepwise process. This system may prove useful in the study of other oncogenes that cause leukemia.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gishizky, M L -- Witte, O N -- New York, N.Y. -- Science. 1992 May 8;256(5058):836-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Molecular Genetics, University of California, Los Angeles 90024.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1375394" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bone Marrow/drug effects ; Bone Marrow Cells ; Cell Differentiation/drug effects ; Cell Division/drug effects ; Cells, Cultured ; Clone Cells ; Drug Resistance, Microbial/genetics ; Fluorouracil/pharmacology ; Fusion Proteins, bcr-abl/*genetics ; Hematopoietic Cell Growth Factors/pharmacology ; Hematopoietic Stem Cells/*cytology/drug effects/physiology ; Humans ; Interleukin-3/pharmacology ; Macrophages/cytology/drug effects ; Mast Cells/cytology/drug effects ; Mice ; Rats ; Retroviridae/genetics ; Stem Cell Factor ; Transfection
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    Production of the Alzheimer amyloid beta protein by normal proteolytic processing (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-10-02
    Description: The 4-kilodalton (39 to 43 amino acids) amyloid beta protein (beta AP), which is deposited as amyloid in the brains of patients with Alzheimer's diseases, is derived from a large protein, the amyloid beta protein precursor (beta APP). Human mononuclear leukemic (K562) cells expressing a beta AP-bearing, carboxyl-terminal beta APP derivative released significant amounts of a soluble 4-kilodalton beta APP derivative essentially identical to the beta AP deposited in Alzheimer's disease. Human neuroblastoma (M17) cells transfected with constructs expressing full-length beta APP and M17 cells expressing only endogenous beta APP also released soluble 4-kilodalton beta AP, and a similar, if not identical, fragment was readily detected in cerebrospinal fluid from individuals with Alzheimer's disease and normal individuals. Thus cells normally produce and release soluble 4-kilodalton beta AP that is essentially identical to the 4-kilodalton beta AP deposited as insoluble amyloid fibrils in Alzheimer's disease.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shoji, M -- Golde, T E -- Ghiso, J -- Cheung, T T -- Estus, S -- Shaffer, L M -- Cai, X D -- McKay, D M -- Tintner, R -- Frangione, B -- AG05891/AG/NIA NIH HHS/ -- AG06656/AG/NIA NIH HHS/ -- AR02594/AR/NIAMS NIH HHS/ -- New York, N.Y. -- Science. 1992 Oct 2;258(5079):126-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurology, Gunma University, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1439760" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/*cerebrospinal fluid ; Amino Acid Sequence ; Amyloid beta-Peptides/*biosynthesis ; Amyloid beta-Protein Precursor/metabolism ; Animals ; Base Sequence ; Cell Line ; Immunoblotting ; Leukemia, Myeloid/*metabolism ; Molecular Sequence Data ; Neuroblastoma/*metabolism ; Transfection
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    Calcium-regulated phosphorylation within the leucine zipper of C/EBP beta (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-04-17
    Description: Alterations in intracellular calcium levels activate several signal transduction pathways resulting in distinct patterns of gene expression. Here, a pathway for calcium-mediated signals is demonstrated that involves C/EBP beta, a member of the bZip family of transcription factors. In pituitary cells C/EBP beta was phosphorylated in response to increased intracellular calcium concentrations as a consequence of the activation of a calcium-calmodulin-dependent protein kinase. Phosphorylation of serine at position 276 within the leucine zipper of C/EBP beta appeared to confer calcium-regulated transcriptional stimulation of a promoter that contained binding sites for C/EBP beta.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wegner, M -- Cao, Z -- Rosenfeld, M G -- New York, N.Y. -- Science. 1992 Apr 17;256(5055):370-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, University of California, San Diego, La Jolla 92093-0648.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1314426" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Binding Sites ; CCAAT-Enhancer-Binding Proteins ; Calcimycin/pharmacology ; Calcium/*pharmacology ; Calcium-Calmodulin-Dependent Protein Kinases ; Cell Line ; DNA/chemistry/genetics/metabolism ; DNA-Binding Proteins/chemistry/*metabolism ; Enzyme Activation/drug effects ; *Leucine Zippers ; Molecular Sequence Data ; Nuclear Proteins/chemistry/*metabolism ; Phosphorylation ; Phosphoserine/metabolism ; Pituitary Gland/metabolism ; Protein Kinases/metabolism ; Signal Transduction/drug effects ; Transcription Factors/chemistry/*metabolism ; Transcription, Genetic/drug effects ; Transfection
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    Transactivation by AP-1 is a molecular target of T cell clonal anergy (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-08-21
    Description: Anergy is a mechanism of T lymphocyte tolerance induced by antigen receptor stimulation in the absence of co-stimulation. Anergic T cells were shown to have a defect in antigen-induced transcription of the interleukin-2 gene. Analysis of the promoter indicated that the transcription factor AP-1 and its corresponding cis element were specifically down-regulated. Exposure of anergic T cells to interleukin-2 restored both antigen responsiveness and activity of the AP-1 element.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kang, S M -- Beverly, B -- Tran, A C -- Brorson, K -- Schwartz, R H -- Lenardo, M J -- New York, N.Y. -- Science. 1992 Aug 21;257(5073):1134-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Immunology, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1509265" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigen-Presenting Cells/immunology ; Antigens/*immunology ; Base Sequence ; Binding Sites ; Blotting, Northern ; Cell Line ; Concanavalin A/pharmacology ; *Gene Expression Regulation ; *Immune Tolerance ; Interleukin-2/*genetics/pharmacology ; Mice ; Molecular Sequence Data ; Mutation ; Promoter Regions, Genetic/genetics ; Proto-Oncogene Proteins c-jun/*physiology ; RNA, Messenger/metabolism ; Receptors, Antigen, T-Cell/immunology ; T-Lymphocytes/*immunology ; Transcription, Genetic ; Transfection
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  • 37
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    Deficient hippocampal long-term potentiation in alpha-calcium-calmodulin kinase II mutant mice (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-07-10
    Description: As a first step in a program to use genetically altered mice in the study of memory mechanisms, mutant mice were produced that do not express the alpha-calcium-calmodulin-dependent kinase II (alpha-CaMKII). The alpha-CaMKII is highly enriched in postsynaptic densities of hippocampus and neocortex and may be involved in the regulation of long-term potentiation (LTP). Such mutant mice exhibited mostly normal behaviors and presented no obvious neuroanatomical defects. Whole cell recordings reveal that postsynaptic mechanisms, including N-methyl-D-aspartate (NMDA) receptor function, are intact. Despite normal postsynaptic mechanisms, these mice are deficient in their ability to produce LTP and are therefore a suitable model for studying the relation between LTP and learning processes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Silva, A J -- Stevens, C F -- Tonegawa, S -- Wang, Y -- 5 R01 NS 12961-17/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1992 Jul 10;257(5067):201-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Center for Cancer Research, Cambridge, MA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1378648" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Behavior, Animal/physiology ; Blotting, Northern ; Blotting, Southern ; Calcium-Calmodulin-Dependent Protein Kinases ; Chromosome Mapping ; DNA/analysis ; Electrophysiology ; Female ; Hippocampus/*physiology ; Learning/physiology ; Male ; Mice ; Mice, Inbred BALB C ; Mice, Mutant Strains/*genetics ; Mutagenesis, Site-Directed ; Plasmids ; Protein Kinases/*deficiency/*physiology ; RNA/analysis ; Receptors, N-Methyl-D-Aspartate ; Synapses/physiology ; Transfection
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 38
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    Identification of the Ah receptor nuclear translocator protein (Arnt) as a component of the DNA binding form of the Ah receptor (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-05-22
    Description: The Ah (dioxin) receptor binds a number of widely disseminated environmental pollutants, including 2,3,7,8-tetrachlorodibenzo-p-dioxin (TCDD) and polycyclic aromatic hydrocarbons, and mediates their carcinogenic effects. The ligand-bound receptor activates Cyp 1a1 gene transcription through interaction with specific DNA sequences, termed xenobiotic responsive elements (XREs). The Ah receptor nuclear translocator protein (Arnt) is required for Ah receptor function. Arnt is now shown to be a structural component of the XRE binding form of the Ah receptor. Furthermore, Arnt and the ligand-binding subunit of the receptor were extracted as a complex from the nuclei of cells treated with ligand. Arnt contains a basic helix-loop-helix motif, which may be responsible for interacting with both the XRE and the ligand-binding subunit.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Reyes, H -- Reisz-Porszasz, S -- Hankinson, O -- CA 28868/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1992 May 22;256(5060):1193-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, University of California, Los Angeles 90024.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1317062" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies ; Aryl Hydrocarbon Receptor Nuclear Translocator ; Base Sequence ; Cell Line ; Cells, Cultured ; Cytochrome P-450 Enzyme System/genetics ; DNA/genetics/metabolism ; DNA-Binding Proteins/genetics/isolation & purification/*metabolism ; Humans ; Hydrocarbons/metabolism ; Mice ; Molecular Sequence Data ; Oligodeoxyribonucleotides ; Proteins/genetics/isolation & purification/*metabolism ; Receptors, Aryl Hydrocarbon ; Receptors, Drug/genetics/isolation & purification/*metabolism ; Recombinant Proteins/isolation & purification/metabolism ; Tetrachlorodibenzodioxin/metabolism ; *Transcription Factors ; Transcription, Genetic ; Transfection
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  • 39
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    Participation of tyrosine phosphorylation in the cytopathic effect of human immunodeficiency virus-1 (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-04-24
    Description: Protein tyrosine phosphorylation is a common mechanism of signaling in pathways that regulate T cell receptor-mediated cell activation, cell proliferation, and the cell cycle. Because human immunodeficiency virus (HIV) is though to affect normal cell signaling, tyrosine phosphorylation may be associated with HIV cytopathicity. In both HIV-infected cells and transfected cells that stably express HIV envelope glycoproteins undergoing HIVgp41-induced cell fusion, a 30-kilodalton protein was phosphorylated on tyrosine with kinetics similar to those of syncytium formation and cell death. When tyrosine phosphorylation was inhibited by the protein tyrosine kinase inhibitor herbimycin A, envelope-mediated syncytium formation was coordinately reduced. These studies show that specific intracellular signals, which apparently participate in cytopathicity, are generated by HIV and suggest strategies by which the fusion process might be interrupted.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cohen, D I -- Tani, Y -- Tian, H -- Boone, E -- Samelson, L E -- Lane, H C -- New York, N.Y. -- Science. 1992 Apr 24;256(5056):542-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Immunoregulation, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1570514" target="_blank"〉PubMed〈/a〉
    Keywords: Antigens, CD4/physiology ; Benzoquinones ; Cell Line ; Cytopathogenic Effect, Viral/*physiology ; HIV Envelope Protein gp41/genetics/physiology ; HIV-1/*physiology ; Humans ; Lactams, Macrocyclic ; Phosphoproteins/*metabolism ; Phosphorylation ; Protein-Tyrosine Kinases/antagonists & inhibitors/metabolism ; Quinones/pharmacology ; Receptors, Antigen, T-Cell/physiology ; Rifabutin/analogs & derivatives ; Signal Transduction/*physiology ; T-Lymphocytes/microbiology/*physiology ; Transfection ; Tyrosine/*metabolism ; Viral Envelope Proteins/genetics/physiology
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  • 40
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    Processing of the amyloid protein precursor to potentially amyloidogenic derivatives (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-02-07
    Description: The approximately 120-kilodalton amyloid beta protein precursor (beta APP) is processed into a complex set of 8- to 12-kilodalton carboxyl-terminal derivatives that includes potentially amyloidogenic forms with the approximately 4-kilodalton amyloid beta protein (beta AP) at or near their amino terminus. In order to determine if these derivatives are processed in a secretory pathway or by the endosomal-lysosomal system, (i) deletion mutants that produce the normal set of carboxyl-terminal derivatives and shortened secreted derivatives were analyzed and (ii) the effect of inhibitors of endosomal-lysosomal processing was examined. In the secretory pathway, cleavage of the beta APP occurs at a single site within the beta AP to generate one secreted derivative and one nonamyloidogenic carboxyl-terminal fragment, whereas, in the endosomal-lysosomal system, a complex set of carboxyl-terminal derivatives is produced that includes the potentially amyloidogenic forms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Golde, T E -- Estus, S -- Younkin, L H -- Selkoe, D J -- Younkin, S G -- New York, N.Y. -- Science. 1992 Feb 7;255(5045):728-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Neuropathology, Case Western Reserve University School of Medicine, Cleveland, OH 44106.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1738847" target="_blank"〉PubMed〈/a〉
    Keywords: Ammonium Chloride/pharmacology ; Amyloid/*biosynthesis ; Amyloid beta-Protein Precursor/genetics/*metabolism ; Base Sequence ; Cell Line ; Endopeptidases/metabolism ; Humans ; Leupeptins/pharmacology ; Lysosomes/metabolism ; Molecular Sequence Data ; Mutagenesis ; Peptide Fragments/*metabolism/secretion ; Transfection
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  • 41
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    Alternative forms of Max as enhancers or suppressors of Myc-ras cotransformation (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-04-17
    Description: Max is a basic-helix-loop-helix-leucine zipper protein capable of forming sequence-specific DNA binding complexes with Myc proteins. An alternatively spliced messenger RNA has been identified that encodes a form of Max truncated at the COOH-terminus. This delta Max protein retained the ability to bind to the CACGTG motif in a complex with c-Myc but lacks the nuclear localization signal and the putative regulatory domain of Max. When tested in a myc-ras cotransformation assay in rat embryo fibroblasts, Max suppressed, whereas delta Max enhanced, transformation. Thus, the max gene may encode both a negative and a positive regulator of c-Myc function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Makela, T P -- Koskinen, P J -- Vastrik, I -- Alitalo, K -- New York, N.Y. -- Science. 1992 Apr 17;256(5055):373-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Virology, University of Helsinki, Finland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1566084" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Basic Helix-Loop-Helix Leucine Zipper Transcription Factors ; Basic-Leucine Zipper Transcription Factors ; Binding Sites ; Cell Nucleus/metabolism ; Cell Transformation, Neoplastic/*drug effects/genetics ; DNA/chemistry/metabolism ; DNA-Binding Proteins/genetics/metabolism/*pharmacology ; Fibroblasts ; *Genes, myc ; *Genes, ras ; Humans ; Immunosorbent Techniques ; Molecular Sequence Data ; Polymerase Chain Reaction ; Proto-Oncogene Proteins c-myc/genetics/metabolism ; RNA Splicing ; RNA, Messenger/genetics ; Rats ; Structure-Activity Relationship ; *Transcription Factors ; Transfection
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  • 42
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    Invariant chain peptides in most HLA-DR molecules of an antigen-processing mutant (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-12-11
    Description: Class II major histocompatibility complexes bind peptides in an endosome-like compartment. When the class II null cell line 721.174 was transfected with class II DR3 genes, DR molecules were produced in normal amounts. However, the DR molecules were abnormally conformed and unstable because deletion of an antigen-processing gene had impaired intracellular formation of most class II-peptide complexes. Yet, 70 percent of the DR molecules still bore peptides, 80 percent of which were 21- to 24-amino acid fragments of the class II-associated invariant chain. These peptides were rare on DR3 from control cells. Thus, a defect in the main antigen-processing pathway revealed a process in which DR molecules bind long peptides derived from proteins present in the same compartment.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sette, A -- Ceman, S -- Kubo, R T -- Sakaguchi, K -- Appella, E -- Hunt, D F -- Davis, T A -- Michel, H -- Shabanowitz, J -- Rudersdorf, R -- AI15486/AI/NIAID NIH HHS/ -- AI18634/AI/NIAID NIH HHS/ -- GM37537/GM/NIGMS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1992 Dec 11;258(5089):1801-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Genetics, University of Wisconsin, Madison 53706.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1465617" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Binding Sites ; Cell Line ; Gene Deletion ; *Genes, MHC Class II ; HLA-DR Antigens/*genetics/*metabolism ; HLA-DR3 Antigen/*genetics/metabolism ; Humans ; Kinetics ; Macromolecular Substances ; Molecular Sequence Data ; Peptides/*metabolism ; Transfection
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  • 43
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    Acquisition of myogenic specificity by replacement of three amino acid residues from MyoD into E12 (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-05-15
    Description: The basic helix-loop-helix (bHLH) protein MyoD is a transcription factor that is important for the induction of the myogenic phenotype. The DNA binding basic region (13 amino acids) is necessary for recognition of the consensus MyoD binding site, for transcriptional activation, and for conversion of fibroblasts to muscle. In contrast, the non-tissue-specific bHLH protein E12 can bind to the MyoD binding site but does not induce myogenesis. Here, it is shown that only two amino acids in the MyoD basic region and a single amino acid from the junction, which separates the basic region and helix 1, are sufficient for myogenic specificity when substituted into the corresponding region of E12. These findings suggest that the recognition of particular determinants in the basic region is required for conversion of fibroblasts to muscle.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davis, R L -- Weintraub, H -- New York, N.Y. -- Science. 1992 May 15;256(5059):1027-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute Laboratory, Fred Hutchinson Cancer Research Center, Seattle, WA 98104.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1317057" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; Binding Sites ; Cell Differentiation ; Cell Line ; DNA/metabolism ; DNA Probes ; DNA-Binding Proteins/chemistry/metabolism/pharmacology ; Fibroblasts/cytology ; Fluorescent Antibody Technique ; Molecular Sequence Data ; Muscle Proteins/chemistry/genetics/*physiology ; Muscles/*cytology ; MyoD Protein ; Protein Conformation ; Structure-Activity Relationship ; Transcription Factors/chemistry/metabolism/pharmacology ; Transfection
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  • 44
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    Identification of a prenylation site in delta virus large antigen (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-05-29
    Description: During replication, hepatitis delta virus (HDV) switches from production of small to large delta antigen. Both antigen isoforms have an HDV genome binding domain and are packaged into hepatitis B virus (HBV)-derived envelopes but differ at their carboxy termini. The large antigen was shown to contain a terminal CXXX box and undergo prenylation. The large, but not the small, antigen formed secreted particles when expressed singly with HBV surface antigen. Mutation of Cys211 in the CXXX box of the large antigen abolished both prenylation and particle formation, suggesting that this site is important for virion morphogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Glenn, J S -- Watson, J A -- Havel, C M -- White, J M -- New York, N.Y. -- Science. 1992 May 29;256(5061):1331-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of California, San Francisco 94143-0450.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1598578" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Amino Acid Sequence ; Animals ; Antigens, Viral/genetics/isolation & purification/*metabolism ; Cell Line ; Cysteine ; Hepatitis Delta Virus/genetics/metabolism/*physiology ; Hepatitis delta Antigens ; Mevalonic Acid/*metabolism ; Mice ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Proline/metabolism ; Protein Biosynthesis ; RNA, Messenger/metabolism ; Rabbits ; Reticulocytes/metabolism ; Serine ; Transfection ; Virus Replication
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  • 45
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    Rapamycin-induced inhibition of the 70-kilodalton S6 protein kinase (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-08-14
    Description: The immunosuppressant rapamycin inhibited proliferation of the H4IIEC hepatoma cell line. Rapamycin, but not its structural analog FK506, also inhibited the basal and insulin-stimulated activity of the p70 ribosomal protein S6 kinase. By contrast, insulin stimulation of the p85 Rsk S6 kinase and mitogen-activated protein (MAP) kinase activity were unaffected by drug. Rapamycin treatment of COS cells transfected with recombinant p70 S6 kinase completely inhibited the appearance of the hyperphosphorylated form of p70 S6 kinase concomitant with the inhibition of enzyme activity toward 40S subunits. Thus, rapamycin inhibits a signal transduction element that is necessary for the activation of p70 S6 kinase and mitogenesis but unnecessary for activation of p85 Rsk S6 kinase or MAP kinase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Price, D J -- Grove, J R -- Calvo, V -- Avruch, J -- Bierer, B E -- P01 CA39542/CA/NCI NIH HHS/ -- R01 DK17776/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1992 Aug 14;257(5072):973-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Diabetes Unit, Massachusetts General Hospital, Boston.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1380182" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium-Calmodulin-Dependent Protein Kinases ; Cell Line ; Chromatography, Ion Exchange ; Cyclosporine/pharmacology ; Immunosuppressive Agents/*pharmacology ; Insulin/pharmacology ; Kinetics ; Liver Neoplasms, Experimental ; Polyenes/*pharmacology ; *Protein Kinase Inhibitors ; Protein Kinases/genetics/isolation & purification/*metabolism ; Recombinant Proteins/antagonists & inhibitors/isolation & purification ; Ribosomal Protein S6 Kinases ; Ribosomes/enzymology ; Sirolimus ; Tacrolimus/pharmacology ; Tetradecanoylphorbol Acetate/pharmacology ; Transfection
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  • 46
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    A point mutation of the alpha 2-adrenoceptor that blocks coupling to potassium but not calcium currents (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-08-14
    Description: The alpha 2A-adrenergic receptor (adrenoceptor) was stably expressed in AtT20 mouse pituitary tumor cells; adrenoceptor agonists inhibited adenylyl cyclase, inhibited voltage-dependent calcium currents, and increased inwardly rectifying potassium currents. An aspartic acid residue (Asp79) highly conserved among guanine nucleotide-binding protein (G protein)-coupled receptors was mutated to asparagine; in cells transfected with the mutant alpha 2-receptor, agonists inhibited adenylyl cyclase and calcium currents but did not increase potassium currents. Because distinct G proteins appear to couple adrenoceptors to potassium and calcium currents, the present findings suggest that the mutant alpha 2-adrenoceptor cannot achieve the conformation necessary to activate G proteins that mediate potassium channel activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Surprenant, A -- Horstman, D A -- Akbarali, H -- Limbird, L E -- New York, N.Y. -- Science. 1992 Aug 14;257(5072):977-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Vollum Institute, Oregon Health Sciences University, Portland 97201.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1354394" target="_blank"〉PubMed〈/a〉
    Keywords: Adrenergic alpha-Agonists/pharmacology ; Animals ; Asparagine ; Aspartic Acid ; Brimonidine Tartrate ; Calcium Channels/drug effects/metabolism/*physiology ; Cell Line ; Clonidine/pharmacology ; GTP-Binding Proteins/metabolism ; Membrane Potentials/drug effects ; *Mutagenesis, Site-Directed ; Potassium Channels/drug effects/metabolism/*physiology ; Quinoxalines/pharmacology ; Receptors, Adrenergic, alpha/drug effects/metabolism/*physiology ; Receptors, Neurotransmitter/drug effects/*physiology ; Receptors, Somatostatin ; Recombinant Proteins/drug effects/metabolism ; Somatostatin/metabolism/pharmacology ; Transfection
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  • 47
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    A mutation in the POU-homeodomain of Pit-1 responsible for combined pituitary hormone deficiency (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-08-21
    Description: Pit-1 is a pituitary-specific transcription factor responsible for pituitary development and hormone expression in mammals. Mutations in the gene encoding Pit-1 have been found in two dwarf mouse strains displaying hypoplasia of growth hormone, prolactin, and thyroid-stimulating, hormone-secreting cell types in the anterior pituitary. A point mutation in this gene was identified on one allele in a patient with combined pituitary hormone deficiency. Mutant Pit-1 binds DNA normally but acts as a dominant inhibitor of Pit-1 action in the pituitary.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Radovick, S -- Nations, M -- Du, Y -- Berg, L A -- Weintraub, B D -- Wondisford, F E -- New York, N.Y. -- Science. 1992 Aug 21;257(5073):1115-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pediatrics, Rainbow Babies and Childrens Hospital, Cleveland, OH.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1509262" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Base Sequence ; Binding Sites ; DNA/chemistry/genetics/metabolism ; DNA-Binding Proteins/chemistry/*genetics ; Growth Hormone/deficiency/genetics ; Humans ; Molecular Sequence Data ; *Mutation ; Pituitary Gland, Anterior/metabolism/pathology ; Pituitary Hormones/*deficiency ; Polymerase Chain Reaction ; Prolactin/deficiency/genetics ; Promoter Regions, Genetic ; Thyrotropin/deficiency/genetics ; Transcription Factor Pit-1 ; Transcription Factors/chemistry/*genetics ; Transfection
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  • 48
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    Alzheimer's disease: a cell biological perspective (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-05-08
    Description: An almost bewildering number of findings concerning Alzheimer's disease mask the significant recent progress in understanding the molecular basis of some inherited forms of this disease and the proteolytic processing of proteins related to the disease. Alzheimer's disease is an amyloidosis, a condition in which certain proteins or protein fragments precipitate in various tissues as amyloid, fibrillar aggregates with a beta-pleated sheet conformation. Alzheimer's is also characterized by neuritic lesions and cell death. Some rare forms of the disease are now known to arise from a mutation in an amyloidogenic protein. Another recent insight is the discovery of an endosomal-lysosomal processing pathway capable of generating protein fragments that can deposit extracellularly as amyloid fibrils. Key future directions for cellular-based research in Alzheimer's disease include the study of membrane trafficking and the passage of intracellular material to the extracellular milieu, molecular signaling among intracellular compartments, the interaction between organelles and the neuronal cytoskeleton, and the nature of cytoskeletal reorganization after neuronal injury.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kosik, K S -- AG06601/AG/NIA NIH HHS/ -- NS29031/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1992 May 8;256(5058):780-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Harvard Medical School, Department of Medicine, Brigham and Women's Hospital, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1589757" target="_blank"〉PubMed〈/a〉
    Keywords: Alzheimer Disease/*genetics/pathology ; Amino Acid Sequence ; Amyloid beta-Protein Precursor/*genetics ; Animals ; Brain/pathology ; Glycosylation ; Humans ; Molecular Sequence Data ; Neurites/ultrastructure ; Neurofibrillary Tangles/ultrastructure ; Transfection
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  • 49
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    Heteromeric NMDA receptors: molecular and functional distinction of subtypes (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-05-22
    Description: The N-methyl D-aspartate (NMDA) receptor subtype of glutamate-gated ion channels possesses high calcium permeability and unique voltage-dependent sensitivity to magnesium and is modulated by glycine. Molecular cloning identified three complementary DNA species of rat brain, encoding NMDA receptor subunits NMDAR2A (NR2A), NR2B, and NR2C, which are 55 to 70% identical in sequence. These are structurally related, with less than 20% sequence identity, to other excitatory amino acid receptor subunits, including the NMDA receptor subunit NMDAR1 (NR1). Upon expression in cultured cells, the new subunits yielded prominent, typical glutamate- and NMDA-activated currents only when they were in heteromeric configurations with NR1. NR1-NR2A and NR1-NR2C channels differed in gating behavior and magnesium sensitivity. Such heteromeric NMDA receptor subtypes may exist in neurons, since NR1 messenger RNA is synthesized throughout the mature rat brain, while NR2 messenger RNA show a differential distribution.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Monyer, H -- Sprengel, R -- Schoepfer, R -- Herb, A -- Higuchi, M -- Lomeli, H -- Burnashev, N -- Sakmann, B -- Seeburg, P H -- New York, N.Y. -- Science. 1992 May 22;256(5060):1217-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Molecular Biology, University of Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1350383" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Brain/*physiology ; Cell Line ; Cloning, Molecular ; DNA/genetics ; Glutamates/pharmacology ; Glutamic Acid ; Glycine/pharmacology ; Macromolecular Substances ; Magnesium/pharmacology ; Membrane Potentials/drug effects ; Molecular Sequence Data ; Multigene Family ; N-Methylaspartate/pharmacology ; Oligonucleotide Probes ; Organ Specificity ; Peptides ; RNA, Messenger/genetics/metabolism ; Rats ; Receptors, N-Methyl-D-Aspartate/*genetics/*metabolism ; Recombinant Proteins/drug effects/metabolism ; Sequence Homology, Nucleic Acid ; Transfection
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  • 50
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    Isolation of a complementary DNA that encodes the mammalian splicing factor SC35 (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-04-24
    Description: The mammalian splicing factor SC35 is required for the first step in the splicing reaction and for spliceosome assembly. The cloning and characterization of a complementary DNA encoding this protein revealed that it is a member of a family of splicing factors that includes mammalian SF2/ASF. This family of proteins is characterized by the presence of a ribonucleoprotein (RNP)-type RNA binding motif and a carboxyl-terminal serine-arginine-rich (SR) domain. A search of the DNA sequence database revealed that the thymus-specific exon (ET) of the c-myb proto-oncogene is encoded on the antisense strand of the SC35 gene.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fu, X D -- Maniatis, T -- GM42231/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 1992 Apr 24;256(5056):535-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, Harvard University, Cambridge, MA 02138.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1373910" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Baculoviridae/genetics ; Base Sequence ; Binding Sites ; Blotting, Northern ; Cell Line ; Cloning, Molecular ; Codon ; DNA/chemistry/*isolation & purification ; Exons ; Humans ; Molecular Sequence Data ; *Nuclear Proteins ; Proteins/chemistry/*genetics ; Proto-Oncogene Proteins/genetics ; Proto-Oncogene Proteins c-myb ; RNA/metabolism ; *RNA Splicing ; *Ribonucleoproteins ; Sequence Homology, Nucleic Acid ; Transfection
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Transcription factor loading on the MMTV promoter: a bimodal mechanism for promoter activation (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-03-20
    Description: The mouse mammary tumor virus (MMTV) promoter attains a phased array of six nucleosomes when introduced into rodent cells. This architecture excludes nuclear factor 1/CCAAT transcription factor (NF1/CTF) from the promoter before glucocorticoid treatment and hormone-dependent access of nucleolytic agents to promoter DNA. In contrast, when the promoter was transiently introduced into cells, NF1/CTF was bound constitutively and nucleolytic attack was hormone-independent. Thus, induction at this promoter was a bimodal process involving receptor-dependent remodeling of chromatin that allows NF1/CTF loading and direct receptor-mediated recruitment of additional transcription factors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Archer, T K -- Lefebvre, P -- Wolford, R G -- Hager, G L -- New York, N.Y. -- Science. 1992 Mar 20;255(5051):1573-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Hormone Action and Oncogenesis Section, Laboratory of Molecular Virology, National Cancer Institute, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1347958" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; *CCAAT-Enhancer-Binding Proteins ; DNA, Viral/physiology ; DNA-Binding Proteins/physiology ; Dexamethasone/pharmacology ; *Gene Expression Regulation, Viral ; Glucocorticoids/physiology ; In Vitro Techniques ; Mammary Tumor Virus, Mouse/*genetics ; Molecular Sequence Data ; NFI Transcription Factors ; Nuclear Proteins ; Nucleosomes/physiology ; Polymorphism, Restriction Fragment Length ; Promoter Regions, Genetic/*physiology ; Restriction Mapping ; Rodentia/*genetics ; Transcription Factors/*physiology ; Transfection ; Y-Box-Binding Protein 1
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    Cloning of the gamma chain of the human IL-2 receptor (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-07-17
    Description: A third subunit, the gamma chain, of the human interleukin-2 receptor (IL-2R) was identified, and a complementary DNA clone encoding this member of the cytokine receptor family was isolated. The gamma chain is necessary for the formation of the high- and intermediate-affinity receptors, which consists of alpha beta gamma heterotrimers and beta gamma heterodimers, respectively. The IL-2R on murine fibroblastoid cells can be internalized after binding IL-2 only if the gamma chain is present; alpha and beta are insufficient for internalization. Thus, the gamma chain is an indispensable component of the functional IL-2R.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Takeshita, T -- Asao, H -- Ohtani, K -- Ishii, N -- Kumaki, S -- Tanaka, N -- Munakata, H -- Nakamura, M -- Sugamura, K -- New York, N.Y. -- Science. 1992 Jul 17;257(5068):379-82.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, Tohoku University School of Medicine, Sendai, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1631559" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Blotting, Northern ; Chromosome Mapping ; Cloning, Molecular ; Humans ; Interleukin-2/metabolism ; Molecular Sequence Data ; RNA, Messenger/biosynthesis ; Receptors, Interleukin-2/*genetics/isolation & purification/physiology ; Sequence Homology, Nucleic Acid ; Transcription, Genetic ; Transfection
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    SV2, a brain synaptic vesicle protein homologous to bacterial transporters (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-08-28
    Description: Synaptic vesicle protein 2 (SV2) is a membrane glycoprotein specifically localized to secretory vesicles in neurons and endocrine cells. As a first step toward understanding the function of SV2 in neural secretion, a rat brain complementary DNA (cDNA) that encodes SV2 was isolated and characterized. Analyses of this cDNA predict that SV2 contains 12 transmembrane domains. The NH2-terminal half of the protein shows significant amino acid sequence identity to a family of bacterial proteins that transport sugars, citrate, and drugs. Expression of the SV2 cDNA in COS cells yielded a high level of SV2-like immunoreactivity distributed in a reticular and punctate pattern, which suggests localization to intracellular membranes. Its localization to vesicles, predicted membrane topology, and sequence identity to known transporters suggest that SV2 is a synaptic vesicle-specific transporter.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bajjalieh, S M -- Peterson, K -- Shinghal, R -- Scheller, R H -- New York, N.Y. -- Science. 1992 Aug 28;257(5074):1271-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Stanford University, CA 94305.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1519064" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Bacterial Proteins/genetics ; Brain/*metabolism ; Carrier Proteins/genetics ; DNA/isolation & purification ; Electrophoresis, Polyacrylamide Gel ; Fungal Proteins/genetics ; Membrane Glycoproteins/*genetics ; Molecular Sequence Data ; Nerve Tissue Proteins/*genetics ; Polymerase Chain Reaction ; Rats ; Sequence Homology, Nucleic Acid ; Transfection
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    A critical role for conserved residues in the cleft of HLA-A2 in presentation of a nonapeptide to T cells (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-08-14
    Description: The peptide binding cleft of the class I human histocompatibility antigen, HLA-A2, contains conserved amino acid residues clustered in the two ends of the cleft in pockets A and F as well as polymorphic residues. The function of two conserved tyrosines in the A pocket was investigated by mutating them to phenylalanines and of a conserved tyrosine and threonine in the F pocket by mutating them to phenylalanine and valine, respectively. Presentation of influenza virus peptides and of intact virus to cytolytic T lymphocytes (CTLs) was then examined. The magnitude of the reduction seen by the mutation of the two tyrosines in the A pocket suggests that hydrogen bonds involving them have a critical function in the binding of the NH2-terminal NH3+ of the peptide nonamer and possibly of all bound peptide nonamers. In contrast, the mutations in the F pocket had no effect on CTL recognition.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Latron, F -- Pazmany, L -- Morrison, J -- Moots, R -- Saper, M A -- McMichael, A -- Strominger, J L -- AI 20182/AI/NIAID NIH HHS/ -- CA 47554/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1992 Aug 14;257(5072):964-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Dana-Farber Cancer Institute, Harvard Medical School, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1380181" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; B-Lymphocytes/immunology ; Binding Sites ; Cell Line ; Cloning, Molecular ; Epitopes/immunology/metabolism ; HLA-A2 Antigen/chemistry/genetics/*metabolism ; Influenza A virus ; Kinetics ; Models, Molecular ; Mutagenesis, Site-Directed ; Oligopeptides/immunology/*metabolism ; Protein Conformation ; Recombinant Proteins/chemistry/metabolism ; T-Lymphocytes, Cytotoxic/*immunology ; Transfection ; Viral Proteins/metabolism
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    Functional modulation of GABAA receptors by cAMP-dependent protein phosphorylation (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-07-31
    Description: gamma-Aminobutyric acidA (GABAA) receptors are ligand-gated ion channels that mediate inhibitory synaptic transmission in the central nervous system. The role of protein phosphorylation in the modulation of GABAA receptor function was examined with cells transiently transfected with GABAA receptor subunits. GABAA receptors consisting of the alpha 1 and beta 1 or the alpha 1, beta 1, and gamma 2 subunits were directly phosphorylated on the beta 1 subunit by adenosine 3',5'-monophosphate (cAMP)-dependent protein kinase (PKA). The phosphorylation decreased the amplitude of the GABA response of both receptor types and the extent of rapid desensitization of the GABAA receptor that consisted of the alpha 1 and beta 1 subunits. Site-specific mutagenesis of the serine residue phosphorylated by PKA completely eliminated the PKA phosphorylation and modulation of the GABAA receptor. In primary embryonic rat neuronal cell cultures, a similar regulation of GABAA receptors by PKA was observed. These results demonstrate that the GABAA receptor is directly modulated by protein phosphorylation and suggest that neurotransmitters or neuropeptides that regulate intracellular cAMP levels may modulate the responses of neurons to GABA and consequently have profound effects on synaptic excitability.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Moss, S J -- Smart, T G -- Blackstone, C D -- Huganir, R L -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1992 Jul 31;257(5070):661-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neuroscience, Howard Hughes Medical Institute, Johns Hopkins University School of Medicine, Baltimore, MD 21205.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1323140" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Cells, Cultured ; Colforsin/pharmacology ; Cyclic AMP/*pharmacology ; Electric Conductivity ; Immunosorbent Techniques ; Kinetics ; Mice ; Mutagenesis, Site-Directed ; Neurons/drug effects/physiology ; Peptide Mapping ; Phosphorylation ; Protein Kinases/*metabolism ; Rats ; Receptors, GABA-A/genetics/*physiology ; Recombinant Proteins/physiology ; Transfection ; Zinc/pharmacology ; gamma-Aminobutyric Acid/pharmacology
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    Rational design of potent antagonists to the human growth hormone receptor (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-06-19
    Description: A hybrid receptor was constructed that contained the extracellular binding domain of the human growth hormone (hGH) receptor linked to the transmembrane and intracellular domains of the murine granulocyte colony-stimulating factor receptor. Addition of hGH to a myeloid leukemia cell line (FDC-P1) that expressed the hybrid receptor caused proliferation of these cells. The mechanism for signal transduction of the hybrid receptor required dimerization because monoclonal antibodies to the hGH receptor were agonists whereas their monovalent fragments were not. Receptor dimerization occurs sequentially--a receptor binds to site 1 on hGH, and then a second receptor molecule binds to site 2 on hGH. On the basis of this sequential mechanism, which may occur in many other cytokine receptors, inactive hGH analogs were designed that were potent antagonists to hGH-induced cell proliferation. Such antagonists could be useful for treating clinical conditions of hGH excess, such as acromegaly.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fuh, G -- Cunningham, B C -- Fukunaga, R -- Nagata, S -- Goeddel, D V -- Wells, J A -- New York, N.Y. -- Science. 1992 Jun 19;256(5064):1677-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Protein Engineering, Genentech, Inc., South San Francisco, CA 94080.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1535167" target="_blank"〉PubMed〈/a〉
    Keywords: Antibodies, Monoclonal ; Cell Division/drug effects ; Cell Line ; DNA Replication/drug effects ; Dose-Response Relationship, Drug ; Growth Hormone/analysis/physiology ; Humans ; Models, Molecular ; Receptors, Granulocyte Colony-Stimulating Factor/physiology ; Receptors, Somatotropin/*physiology ; Signal Transduction/physiology ; Transfection
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    At age 2, gene therapy enters a growth phase (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-10-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Thompson, L -- New York, N.Y. -- Science. 1992 Oct 30;258(5083):744-6.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1472258" target="_blank"〉PubMed〈/a〉
    Keywords: Acquired Immunodeficiency Syndrome/therapy ; Adenosine Deaminase/deficiency ; DNA, Viral/genetics ; Genetic Therapy/*trends ; Genetic Vectors ; HIV/genetics ; Humans ; Immunologic Deficiency Syndromes/therapy ; National Institutes of Health (U.S.) ; Neoplasms/therapy ; Retroviridae/genetics ; Transfection ; United States
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    Prevention of programmed cell death of sympathetic neurons by the bcl-2 proto-oncogene (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-10-09
    Description: Approximately half of the neurons produced during embryogenesis normally die before adulthood. Although target-derived neurotrophic factors are known to be major determinants of programmed cell death--apoptosis--the molecular mechanisms by which trophic factors interfere with cell death regulation are largely unknown. Overexpression of the bcl-2 proto-oncogene in cultured sympathetic neurons has now been shown to prevent apoptosis normally induced by deprivation of nerve growth factor. This finding, together with the previous demonstration of bcl-2 expression in the nervous system, suggests that the Bcl-2 protein may be a major mediator of the effects of neurotrophic factors on neuronal survival.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Garcia, I -- Martinou, I -- Tsujimoto, Y -- Martinou, J C -- CA-50551/CA/NCI NIH HHS/ -- CA-51864/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1992 Oct 9;258(5080):302-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Centre Medical Universitaire, Geneva, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1411528" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Apoptosis/*genetics ; Cell Death/*genetics ; Cells, Cultured ; Ganglia, Sympathetic/cytology ; Gene Expression ; Humans ; Nerve Growth Factors/physiology ; Neurons/*physiology ; Proto-Oncogene Proteins/*genetics ; Proto-Oncogene Proteins c-bcl-2 ; Rats ; Sympathetic Nervous System/*cytology ; Transfection
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    Reciprocal regulation of adipogenesis by Myc and C/EBP alpha (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-04-17
    Description: 3T3-L1 adipoblasts that express large amounts of c-Myc cannot terminally differentiate, raising the possibility that Myc inhibits the expression of genes that promote adipogenesis. The CCAAT/enhancer binding protein (C/EBP alpha) is induced during 3T3-L1 adipogenesis when cells commit to the differentiation pathway. Transfection of 3T3-L1 adipoblasts with the gene that encodes C/EBP alpha caused overt expression of the adipocyte morphology. Expression of Myc prohibited the normal induction of C/EBP alpha and prevented adipogenesis. Enforced expression of C/EBP alpha overcame the Myc-induced block to differentiation. These results provide a molecular basis for the regulation of adipogenesis and implicate Myc and C/EBP alpha as pivotal controlling elements.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Freytag, S O -- Geddes, T J -- CA51748/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1992 Apr 17;256(5055):379-82.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Biology Research Program, Henry Ford Hospital, Detroit, MI 48202.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1566086" target="_blank"〉PubMed〈/a〉
    Keywords: Adipose Tissue/*cytology/metabolism ; Animals ; Base Sequence ; CCAAT-Enhancer-Binding Proteins ; Cell Differentiation ; Cell Division ; Cell Line ; DNA-Binding Proteins/genetics/*physiology ; *Gene Expression Regulation ; Molecular Sequence Data ; Nuclear Proteins/genetics/*physiology ; Plasmids ; Polymerase Chain Reaction ; Proto-Oncogene Proteins c-myc/genetics/*physiology ; RNA, Messenger/analysis ; Rats ; Transfection
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    An eosinophil-dependent mechanism for the antitumor effect of interleukin-4 (1992)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 1992-07-24
    Description: Murine interleukin-4 (IL-4) exhibits potent antitumor activity when present at the site of tumor cell challenge. Associated with tumor cell death is the appearance of an inflammatory infiltrate comprised predominantly of eosinophils and macrophages, but with few lymphocytes. Antibodies that specifically block the accumulation of granulocytes at the site of inflammation were injected in vivo to define the cell type responsible for the antitumor action of IL-4. These studies implicate eosinophils in IL-4-mediated tumor cytotoxicity. The lymphoid-independent nature of IL-4 action is supported by the analysis of mutant mouse strains with defined lymphocyte immunodeficiencies. The observed regression of established tumor masses by localized IL-4 action provides a rationale for exploring IL-4-mediated tumor killing as a potential therapy for human malignant disorders.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tepper, R I -- Coffman, R L -- Leder, P -- New York, N.Y. -- Science. 1992 Jul 24;257(5069):548-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉MGH Cancer Center, Massachusetts General Hospital, Charlestown 02129.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1636093" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antibodies, Monoclonal/immunology ; Chromatography, Affinity ; Granulocytes/drug effects/pathology ; Inflammation ; Interleukin-4/genetics/isolation & purification/*therapeutic use ; Mice ; Mice, Inbred BALB C ; Nematode Infections/blood/pathology ; Neutrophils/drug effects/immunology/*physiology ; Nippostrongylus ; Plasmacytoma/*immunology/pathology/therapy ; Recombinant Proteins/isolation & purification/therapeutic use ; Transfection
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    Cytochrome b558: the flavin-binding component of the phagocyte NADPH oxidase (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-06-05
    Description: The phagocyte respiratory burst oxidase is a flavin-adenine dinucleotide (FAD)-dependent dehydrogenase and an electron transferase that reduces molecular oxygen to superoxide anion, a precursor of microbicidal oxidants. Several proteins required for assembly of the oxidase have been characterized, but the identity of its flavin-binding component has been unclear. Oxidase activity was reconstituted in vitro with only the purified oxidase proteins p47phox, p67phox, Rac-related guanine nucleotide (GTP)-binding proteins, and membrane-bound cytochrome b558. The reconstituted oxidase required added FAD, and FAD binding was localized to cytochrome b558. Alignment of the amino acid sequence of the beta subunit of cytochrome b558 (gp91phox) with other flavoproteins revealed similarities to the nicotinamide adenine dinucleotide phosphate (reduced) (NADPH)-binding domains. Thus flavocytochrome b558 is the only obligate electron transporting component of the NADPH oxidase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rotrosen, D -- Yeung, C L -- Leto, T L -- Malech, H L -- Kwong, C H -- New York, N.Y. -- Science. 1992 Jun 5;256(5062):1459-62.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Host Defenses, National Institute of Allergy and Infectious Diseases, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1318579" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding Sites ; Cell Line ; Cell-Free System ; Cytochrome b Group/*blood/genetics/isolation & purification ; Ferredoxin-NADP Reductase/genetics/metabolism ; Humans ; Insects ; Molecular Sequence Data ; NADH, NADPH Oxidoreductases/*blood/genetics/isolation & purification ; NADP/metabolism ; NADPH Oxidase ; Neutrophils/*enzymology ; Phagocytes/*enzymology ; Plants/enzymology ; Recombinant Proteins/chemistry/metabolism ; Sequence Homology, Nucleic Acid ; Superoxides/blood ; Transfection
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    The IL-6 signal transducer, gp130: an oncostatin M receptor and affinity converter for the LIF receptor (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-03-13
    Description: Leukemia inhibitory factor (LIF) and interleukin-6 (IL-6) are multifunctional cytokines with many similar activities. LIF is structurally and functionally related to another cytokine, Oncostatin M (OSM), that binds to the high-affinity LIF receptor but not to the low-affinity LIF receptor. A complementary DNA was isolated that encodes the high-affinity converting subunit of the LIF receptor. The converter conferred high-affinity binding of both LIF and OSM when expressed with the low-affinity LIF receptor and is identical to the signal transducing subunit of the IL-6 receptor, gp130. The gp130 subunit alone confers low-affinity binding of OSM when expressed in COS-7 cells. This receptor system resembles the high-affinity receptors for granulocyte-macrophage colony-stimulating factor, IL-3, and IL-5, which share a common subunit.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gearing, D P -- Comeau, M R -- Friend, D J -- Gimpel, S D -- Thut, C J -- McGourty, J -- Brasher, K K -- King, J A -- Gillis, S -- Mosley, B -- New York, N.Y. -- Science. 1992 Mar 13;255(5050):1434-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Immunex Research and Development Corporation, Seattle, WA 98101.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1542794" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Antigens, CD ; Binding, Competitive ; Cell Line, Transformed ; Cytokine Receptor gp130 ; Growth Inhibitors/*metabolism ; Interleukin-6/*metabolism ; Leukemia Inhibitory Factor ; Lymphokines/*metabolism ; Membrane Glycoproteins/*metabolism ; Oncostatin M ; Peptides/*metabolism ; Radioligand Assay ; *Receptors, Cytokine ; Receptors, Immunologic/*metabolism ; Receptors, OSM-LIF ; Recombinant Proteins/metabolism ; Transfection
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    Retinoids selective for retinoid X receptor response pathways (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-12-18
    Description: Retinoids have a broad spectrum of biological activities and are useful therapeutic agents. Their physiological activities are mediated by two types of receptors, the retinoic acid receptors (RARs) and the retinoid X receptors (RXRs). RARs, as well as several related receptors, require heterodimerization with RXRs for effective DNA binding and function. However, in the presence of 9-cis-retinoic acid, a ligand for both RARs and RXRs, RXRs can also form homodimers. A series of retinoids is reported that selectively activates RXR homodimers but does not affect RAR-RXR heterodimers and thus demonstrates that both retinoid response pathways can be independently activated.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lehmann, J M -- Jong, L -- Fanjul, A -- Cameron, J F -- Lu, X P -- Haefner, P -- Dawson, M I -- Pfahl, M -- CA50676/CA/NCI NIH HHS/ -- P01 CA51993/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1992 Dec 18;258(5090):1944-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cancer Center, La Jolla Cancer Research Foundation, La Jolla, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1335166" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Chloramphenicol O-Acetyltransferase/genetics/metabolism ; Kinetics ; Macromolecular Substances ; Molecular Structure ; Receptors, Cell Surface/drug effects/genetics/*metabolism ; *Receptors, Retinoic Acid ; Recombinant Fusion Proteins/metabolism ; Retinoid X Receptors ; Retinoids/chemistry/*metabolism/pharmacology ; Structure-Activity Relationship ; *Transcription Factors ; Transcription, Genetic ; Transfection ; Tretinoin/metabolism/pharmacology
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    A truncated erythropoietin receptor that fails to prevent programmed cell death of erythroid cells (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-08-21
    Description: A form of the human erythropoietin receptor (EPOR) was identified in which the cytoplasmic region is truncated by alternative splicing. The truncated form of the receptor (EPOR-T) is the most prevalent form of EPOR in early-stage erythroid progenitor cells, but the full-length EPOR (EPOR-F) becomes the most prevalent form in late-stage progenitors. EPOR-T can transduce a mitogenic signal. However, cells transfected with EPOR-T are more prone to programmed cell death than those expressing EPOR-F. EPOR-F may transduce a signal to prevent programmed cell death that is independent of the mitogenic signal, and alternative splicing of the EPOR gene may have an important role in erythropoiesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nakamura, Y -- Komatsu, N -- Nakauchi, H -- New York, N.Y. -- Science. 1992 Aug 21;257(5073):1138-41.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Cell Growth and Differentiation, Tsukuba Life Science Center, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1324524" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Base Sequence ; DNA/chemistry/genetics ; Erythrocyte Aging/*physiology ; Erythroid Precursor Cells/metabolism ; Genetic Vectors ; Humans ; Molecular Sequence Data ; Polymerase Chain Reaction ; RNA Splicing ; RNA, Messenger/genetics ; Receptors, Cell Surface/chemistry/genetics/*physiology ; Receptors, Erythropoietin ; Transfection
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    No requirement for p56lck in the antigen-stimulated clonal deletion of thymocytes (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-07-03
    Description: Activation of protein-tyrosine kinases (PTKs) is required for signal transduction during T cell activation, although the pathway used during thymic selection is unknown. An in vitro system was established in which T cell receptor transgenic thymocytes underwent clonal deletion in response to peptide antigen. The effects of two PTK-specific inhibitors, herbimycin A and genistein, on the clonal deletion of immature thymocytes and the activation of mature thymocytes were examined. Clonal deletion occurred while T cell activation was inhibited and when no p56lck activity was evident. Thus, p56lck is not required for the antigen-stimulated step of clonal deletion of immature thymocytes, and negative selection proceeds via a distinct pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nakayama, K -- Loh, D Y -- New York, N.Y. -- Science. 1992 Jul 3;257(5066):94-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Medicine, Washington University School of Medicine, St. Louis, MO 63110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1621101" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Benzoquinones ; Cells, Cultured ; Chickens ; DNA Replication ; Genistein ; Isoflavones/pharmacology ; L Cells (Cell Line) ; Lactams, Macrocyclic ; *Lymphocyte Activation/drug effects ; Lymphocyte Specific Protein Tyrosine Kinase p56(lck) ; Mice ; Mice, Transgenic ; Ovalbumin/immunology ; Protein-Tyrosine Kinases/antagonists & inhibitors/*metabolism ; Quinones/pharmacology ; Receptors, Antigen, T-Cell/*genetics/immunology ; Rifabutin/analogs & derivatives ; *Signal Transduction ; T-Lymphocyte Subsets/immunology ; T-Lymphocytes/drug effects/*immunology ; Transfection
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    Identification of heregulin, a specific activator of p185erbB2 (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-05-22
    Description: The proto-oncogene designated erbB2 or HER2 encodes a 185-kilodalton transmembrane tyrosine kinase (p185erbB2), whose overexpression has been correlated with a poor prognosis in several human malignancies. A 45-kilodalton protein heregulin-alpha (HRG-alpha) that specifically induced phosphorylation of p185erbB2 was purified from the conditioned medium of a human breast tumor cell line. Several complementary DNA clones encoding related HRGs were identified, all of which are similar to proteins in the epidermal growth factor family. Scatchard analysis of the binding of recombinant HRG to a breast tumor cell line expressing p185erbB2 showed a single high affinity binding site [dissociation constant (Kd) = 105 +/- 15 picomolar]. Heregulin transcripts were identified in several normal tissues and cancer cell lines. The HRGs may represent the natural ligands for p185erbB2.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Holmes, W E -- Sliwkowski, M X -- Akita, R W -- Henzel, W J -- Lee, J -- Park, J W -- Yansura, D -- Abadi, N -- Raab, H -- Lewis, G D -- New York, N.Y. -- Science. 1992 May 22;256(5060):1205-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Protein Chemistry, Genentech, Inc., South San Francisco, CA 94080.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1350381" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Base Sequence ; Breast Neoplasms/genetics ; Cell Line ; Chromatography, High Pressure Liquid ; Codon ; Culture Media ; DNA-Binding Proteins/genetics/isolation & purification/*metabolism ; Epidermal Growth Factor/genetics ; Female ; Glycoproteins/*metabolism ; Humans ; Kinetics ; Molecular Sequence Data ; Neuregulins ; Oligonucleotide Probes ; Phosphorylation ; Protein Conformation ; Protein-Tyrosine Kinases/*genetics ; Proto-Oncogene Proteins/*genetics ; *Proto-Oncogenes ; Receptor, ErbB-2 ; Sequence Homology, Nucleic Acid ; Transfection
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    Activation of T cells by a tyrosine kinase activation domain in the cytoplasmic tail of CD3 epsilon (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-01-03
    Description: The multichain T cell antigen receptor functions by interacting with and activating one or more nonreceptor tyrosine kinases. The cytoplasmic tail of the zeta chain can activate T cells independently of the rest of the receptor complex. The function of the remaining invariant CD3 chains remains unknown. A 22-amino acid region of the cytoplasmic tail of CD3 epsilon was also able to independently activate T cells. Stimulation of T cells by means of the cytoplasmic tails of either zeta or CD3 epsilon resulted in quantitatively distinct patterns of tyrosine phosphorylation, suggesting activation of different biochemical pathways.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Letourneur, F -- Klausner, R D -- New York, N.Y. -- Science. 1992 Jan 3;255(5040):79-82.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Biology and Metabolism Branch, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1532456" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, CD3 ; Antigens, Differentiation, T-Lymphocyte/genetics/*metabolism ; Cell Line ; Cell Membrane/immunology/metabolism ; Chimera ; Clone Cells ; Humans ; Interleukin-2/biosynthesis ; Kinetics ; *Lymphocyte Activation ; Macromolecular Substances ; Mice ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Phosphorylation ; Polymerase Chain Reaction ; Protein-Tyrosine Kinases/genetics/*metabolism ; Receptors, Antigen, T-Cell/genetics/*metabolism ; Receptors, Interleukin-2/genetics/metabolism ; T-Lymphocytes/enzymology/*immunology ; Transfection
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    Identification of a naturally occurring transforming variant of the p65 subunit of NF-kappa B (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-04-17
    Description: Transcription factor NF-kappa B comprises two proteins, p50 and p65, that have sequence similarity to the v-rel oncogene. In primary hematopoietic cell populations an alternatively spliced form of NF-kappa B p65 mRNA was observed that encoded a protein designated p65 delta. Expression of the p65 delta cDNA in Rat-1 fibroblasts resulted in focus formation, anchorage-independent growth in soft agar, and tumor formation in athymic nude mice, effects not obtained with expression of p65 or a p65 delta mutant that contains a disruption within the transcriptional activation domain. Thus, p65 delta, which associated weakly and interfered with DNA binding by p65, may sequester an essential limiting regulatory factor or factors required for NF-kappa B function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Narayanan, R -- Klement, J F -- Ruben, S M -- Higgins, K A -- Rosen, C A -- New York, N.Y. -- Science. 1992 Apr 17;256(5055):367-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Genetics, Hoffmann-LaRoche, Inc., Nutley, NJ 07110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1566083" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Base Sequence ; Binding Sites ; Cell Transformation, Neoplastic/*genetics ; DNA/genetics/metabolism ; Fibroblasts/metabolism ; *Genetic Variation ; Hematopoietic Stem Cells/chemistry ; Humans ; Mice ; Mice, Nude ; Molecular Sequence Data ; NF-kappa B/*genetics ; Neoplasm Transplantation ; Oncogene Proteins v-rel ; Polymerase Chain Reaction ; RNA Splicing ; RNA, Messenger/analysis/genetics ; Rats ; Retroviridae Proteins, Oncogenic/genetics ; Transfection
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    Expression of a ryanodine receptor-Ca2+ channel that is regulated by TGF-beta (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-07-03
    Description: Ryanodine receptors (RyRs) are intracellular channels that release calcium ions from the sarcoplasmic reticulum (SR) in response to either plasma membrane depolarization (in skeletal muscle) or increases in the concentration of intracellular free Ca2+ (in the heart). A gene (beta 4) encoding a ryanodine receptor (similar to, but distinct from, the muscle RyRs) was identified. The beta 4 gene was expressed in all tissues investigated, with the exception of heart. Treatment of mink lung epithelial cells (Mv1Lu) with transforming growth factor beta (TGF-beta) induced expression of the beta 4 gene together with the release of Ca2+ in response to ryanodine (but not in response to caffeine, the other drug active on muscle RyRs). This ryanodine receptor may be important in the regulation of intracellular Ca2+ homeostasis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Giannini, G -- Clementi, E -- Ceci, R -- Marziali, G -- Sorrentino, V -- New York, N.Y. -- Science. 1992 Jul 3;257(5066):91-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉European Molecular Biology Laboratory, Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1320290" target="_blank"〉PubMed〈/a〉
    Keywords: 2-Aminopurine/pharmacology ; Amino Acid Sequence ; Animals ; Calcium/*metabolism ; Calcium Channels/drug effects/physiology ; Cell Line ; Cell Membrane/metabolism ; Cloning, Molecular ; Cycloheximide/pharmacology ; Gene Expression/drug effects ; Mink ; Molecular Sequence Data ; Muscles/*physiology ; RNA, Messenger/genetics/metabolism ; Receptors, Cholinergic/drug effects/*genetics/*physiology ; Ryanodine Receptor Calcium Release Channel ; Sarcoplasmic Reticulum/metabolism ; Sequence Homology, Nucleic Acid ; Tetradecanoylphorbol Acetate/pharmacology ; Transcription, Genetic/drug effects ; Transfection ; Transforming Growth Factor beta/*pharmacology
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    Recovery from hemophilia B Leyden: an androgen-responsive element in the factor IX promoter (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-07-17
    Description: One form of the inherited, X-linked, bleeding disorder, hemophilia B, resolves after puberty. Mutations at -20 and -26 in the clotting factor IX promoter impair transcription by disrupting the binding site for the liver-enriched transcription factor LF-A1/HNF4. The -26 but not the -20 mutation also disrupts an androgen-responsive element, which overlaps the LF-A1/HNF4 site. This explains the improvement seen in patients with the -20 mutation and the failure of the -26 patient to recover.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Crossley, M -- Ludwig, M -- Stowell, K M -- De Vos, P -- Olek, K -- Brownlee, G G -- Wellcome Trust/United Kingdom -- New York, N.Y. -- Science. 1992 Jul 17;257(5068):377-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Chemical Pathology Unit, Sir William Dunn School of Pathology, University of Oxford, United Kingdom.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1631558" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Binding Sites/genetics ; Binding, Competitive ; Cloning, Molecular ; Electrophoresis, Polyacrylamide Gel ; Factor IX/*physiology ; Hemophilia B/*genetics ; Humans ; Molecular Sequence Data ; Mutation ; Promoter Regions, Genetic/*physiology ; Receptors, Androgen/metabolism ; Sequence Homology, Nucleic Acid ; Transcription Factors/genetics/metabolism ; Transcription, Genetic ; Transfection
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    Reversal of the orientation of an integral protein of the mitochondrial outer membrane (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-06-26
    Description: The NH2-terminus of the signal-anchor sequence of an integral, bitopic protein of the outer mitochondrial membrane was extended both in amino acid length (from 11 to 38 amino acids) and net charge (from +4 to +8)--changes that confer on the NH2-terminus characteristics of a strong matrix-targeting signal. The protein was inserted into the outer membrane but in an inverted orientation (Ncyto-Cin). These findings suggest that, in common with other membrane systems, the orientation of a protein in the outer mitochondrial membrane can be determined by a signal that causes retention of the NH2-terminus on the cytosolic side of the membrane.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, J M -- Shore, G C -- New York, N.Y. -- Science. 1992 Jun 26;256(5065):1815-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, McGill University, Montreal, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1615327" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Electrophoresis, Polyacrylamide Gel ; Fungal Proteins/chemistry ; Intracellular Membranes/*chemistry ; Membrane Proteins/*chemistry ; Mitochondria/*ultrastructure ; Molecular Sequence Data ; Plasmids ; Protein Sorting Signals/chemistry ; Rats ; Transfection ; Yeasts
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    Release of Alzheimer amyloid precursor derivatives stimulated by activation of muscarinic acetylcholine receptors (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-10-09
    Description: Altered processing of the amyloid precursor protein (APP) is a central event in the formation of amyloid deposits in the brains of individuals with Alzheimer's disease. To investigate whether cellular APP processing is controlled by cell-surface neurotransmitter receptors, human embryonic kidney (293) cell lines were transfected with the genes for human brain muscarinic acetylcholine receptors. Stimulation of m1 and m3 receptor subtypes with carbachol increased the basal release of APP derivatives within minutes of treatment, indicating that preexisting APP is released in response to receptor activation. Receptor-activated APP release was blocked by staurosporine, suggesting that protein kinases mediate neurotransmitter receptor-controlled APP processing.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nitsch, R M -- Slack, B E -- Wurtman, R J -- Growdon, J H -- New York, N.Y. -- Science. 1992 Oct 9;258(5080):304-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Brain and Cognitive Sciences, Massachusetts Institute of Technology, Cambridge 02139.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1411529" target="_blank"〉PubMed〈/a〉
    Keywords: Alkaloids/pharmacology ; Alzheimer Disease/*metabolism ; Amyloid beta-Protein Precursor/*secretion ; Atropine/pharmacology ; Blotting, Western ; Brain Chemistry ; Carbachol/pharmacology ; Cell Line ; Embryo, Mammalian ; Humans ; Kidney ; Kinetics ; Protein Kinase C/antagonists & inhibitors/metabolism ; Receptors, Muscarinic/drug effects/genetics/*physiology ; Staurosporine ; Transfection
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    Identification of envelope V3 loop as the major determinant of CD4 neutralization sensitivity of HIV-1 (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-07-24
    Description: Laboratory isolates of human immunodeficiency virus type-1 (HIV-1) such as HTLV-IIIB are generally T cell line-tropic and highly sensitive to neutralization by soluble CD4 (sCD4), a potential antiviral agent that is undergoing clinical trial. However, many primary HIV-1 isolates are macrophage-tropic and sCD4-resistant. Envelope V3 loop sequences derived from primary HIV-1 isolates were sufficient to confer on HTLV-IIIB not only the tissue tropism but also the degree of sCD4 neutralization resistance characteristic of their HIV-1 strains of origin. Single amino acid changes in the V3 loop enhanced sCD4 resistance by up to tenfold. These observations suggest that the tissue tropism and sCD4 neutralization sensitivity of HIV-1 isolates are regulated by similar mechanisms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hwang, S S -- Boyle, T J -- Lyerly, H K -- Cullen, B R -- AI28233/AI/NIAID NIH HHS/ -- AI28662/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 1992 Jul 24;257(5069):535-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, Duke University Medical Center, Durham, NC 27710.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1636088" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, CD4/*immunology ; Cell Line ; Cells, Cultured ; Gene Products, gag/*immunology ; HIV Envelope Protein gp120/*immunology ; HIV-1/*immunology/isolation & purification ; Humans ; Kinetics ; Molecular Sequence Data ; Neutralization Tests ; Proviruses/immunology ; T-Lymphocyte Subsets/*immunology ; Transfection ; Virion/immunology
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    Actin-binding protein requirement for cortical stability and efficient locomotion (1992)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1992-01-17
    Description: Three unrelated tumor cell lines derived from human malignant melanomas lack actin-binding protein (ABP), which cross-links actin filaments in vitro and connects these filaments to plasma membrane glycoproteins. The ABP-deficient cells have impaired locomotion and display circumferential blebbing of the plasma membrane. Expression of ABP in one of the lines after transfection restored translocational motility and reduced membrane blebbing. These findings establish that ABP functions to stabilize cortical actin in vivo and is required for efficient cell locomotion.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cunningham, C C -- Gorlin, J B -- Kwiatkowski, D J -- Hartwig, J H -- Janmey, P A -- Byers, H R -- Stossel, T P -- AI 08051/AI/NIAID NIH HHS/ -- AR 38910/AR/NIAMS NIH HHS/ -- HL 19429/HL/NHLBI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 1992 Jan 17;255(5042):325-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Divisions of Experimental Medicine, Brigham & Women's Hospital, Boston, MA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/1549777" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/physiology ; Blotting, Southern ; Cell Line ; Cell Membrane/*physiology/ultrastructure ; Cell Movement/*physiology ; Humans ; Melanoma ; Membrane Glycoproteins/physiology ; Microfilament Proteins/*physiology ; Transfection
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